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Miscellaneous Article

References

Pages 89-98 | Published online: 17 Mar 2010

References

Proceedings and books

  • New Methods for the Analysis of Coagulation Using Chromogenic Substrates, I. Witt. Walter de Gruyter. 1977
  • Progress in Chemical Fibrinolysis and Thrombolysis, J. F. Davidson, R. M. Rowan, M. M. Samama, P. C. Desnoyers. Raven Press. 1978; Vol. 3
  • Progress in Chemical Fibrinolysis and Thrombolysis, J. F. Davidson, V. Cepelák, M. M. Samama, P. C. Desnoyers. Churchill Livingstone. 1979; Vol. 4
  • Enzymes, M. Dixon, E. C. Webb. Longmans Green, London 1964
  • Chromogenic Peptide Substrates: Chemistry and Clinical Usage, M. F. Scully, V. V. Kakkar. Churchill Livingstone. 1979
  • The Physiological Inhibitors of Blood Coagulation and Fibrinolysis, D. Collen, B. Wiman, M. Verstraete. Elsevier North Holland Biomedical Press. 1979
  • Synthetic Substrates in Clinical Blood Coagulation Assays, H. R. Lijnen, D. Collen, M. Verstraete. Martinus Nijhof Publishers. 1980
  • Progress in Chemical Fibrinolysis and Thrombolysis, J. F. Davidson, I. M. Nilsson, B. Åstedt. Churchill Livingstone. 1981; Vol. 5
  • Annals of New York Academy of Science, D. A. Walz, L. E. McCoy, 1981; Vol. 370, Contribution to Hemostasis
  • IUPAC Enzyme Nomenclature, Recommendations (1972) of the International Union of Pure and Applied Chemistry and the International Union of Biochemistry. Elsevier, Amsterdam 1973

Ordinary references

  • Aasen A. O., Amundsen E. Effect of slow intravenous endotoxin infusion on plasma kallikrein-kinin and fibrinolytic enzyme systems in dogs. Eur. surg. Res 1977; 9(suppl. 1)12
  • Aasen A. O., Frølich W., Saugstad O. D., Amundsen E. Plasma kallikrein activity and prekallikrein levels during endotoxin shock in dogs. Eur. surg. Res 1978; 10: 50–62
  • Aasen A. O., Ohlsson K., Larsbraaten M., Amundsen E. Changes in plasminogen levels, plasmin activity and activity of antiplasmins during endotoxin shock in dogs. Eur. surg. Res 1978; 10: 63–72
  • Aasen A. O., Dale J., Ohlsson K., Gallimore M. Effects of slow intravenous administration of endotoxin on blood cells and coagulation in dogs. Eur. surg. Res 1978; 10: 194–205
  • Aasen A. O., Ohlsson K. Release of granulocyte elastase in letal canine endotoxin shock. Hoppe-Seyler's Z. Physiol. Chem 1978; 359: 683–690
  • Aasen A. O., Larsbraaten M. “Immediate” and “time depending” antiplasmin activity in endotoxin shock in dogs. 323–326, In ref. 2
  • Aasen A. O., Gallimore M. J., Lilleaasen P., Lyngaas K., Larsbraaten M., Amundsen E. Changes in antiplasmin and plasmin activities during extreme hemodilution and open heart surgery in dogs. Eur. surg. Res 1979; 11: 145–153
  • Aasen A. O., Erichsen N. Smith, Gallimore M. J., Amundsen E. Studies on components of the plasma kallikrein-kinin system in plasma samples from normal individuals and patients with septic shock. Advances in Shock Res 1980; 4: 1–10
  • Allen R. A. Studies on the human vascular plasminogen activator. 1980, Cell Biology International Reports, 4, No. 3
  • Allen R. A., Pepper D. S. Isolation and properties of human vascular plasminogen activator. Thrombosis & Haemostasis 1981; 45: 43–50
  • Allen R. A. The effect of poly-lysine on the activation of plasminogen. 134–138, In ref. 8
  • Allen R. A. An enhancing effect of poly-lysine on the activation of plasminogen. Thrombosis & Haemostasis 1982; 47: 41–45
  • Allen R. A., Brommer E. J.P., Kluft C. Blood sampling for fibrinolytic studies: comparison of Vacutainerr` and traditional technique. Thrombosis Res 1981; 23: 197–199
  • Alving B. M., Tankersley D. L., Mason B. L., Rossi F., Aronson D. L., Finlayson J. S. Contact-activated factors: Contaminants of immunoglobulin preparations with coagulant and vasoactive properties. J. Lab. Clin. Med 1980; 96: 334–346
  • Amundsen E., Svendsen L., Vefling A. A sensitive photometric method for determination of plasma inhibition towards plasmin and Brinase. Abstract of a paper read at the IVth Int. Congr. Thrombosis and Haemostasis, Vienna, 1973
  • Amundsen E., Svendsen L., Vennerød A. M., Laake K. Determination of plasma kallikrein with a new chromogenic tripeptide derivative. Chemistry and Biology of the Kallikrein-kinin System in Health and Disease, J. J. Pisano, K. F. Austen. DHEW Publication No. (NIH) 76–791, 1976; 215–220
  • Amundsen E., Gallimore M. J., Aasen A. O., Larsbraaten M., Lyngaas K. Activation of human plasma prekallikrein: Influence of activators, activation time and temperature and inhibitors. Thrombosis Res 1978; 13: 625–636
  • Amundsen E., Gallimore M. J., Aasen A. O., Lyngaas M., Larsbraaten M., Smith-Erichsen N. On the discrepancy between functional activities and immunological levels of plasma protease inhibitors during septicemia. Microvascular Res 1979; 18: 293
  • Amundsen E., Aasen A. O., Gallimore M. J., Larsbraaten M., Lyngaas M. The plasma-kallikrein-kinin system in endotoxin shock in dogs. 72–83, In ref. 5
  • Amundsen E., Aasen A. O., Gallimore M. J., Larsbraaten M., Lyngaas K., Engeseth A. Plasma prekallikrein activities and Cl-esterase inhibitor levels in plasma samples from cancer patients and healthy individuals. 406–410, In ref. 3
  • Angelkort B., Kienel R. Zuverlässigkeit und Aussagekraft der photometrischen Bestimmung von Plasminogen, Plasmin und Antiplasmin mit der chromogenen Substanz S-2251. Prostaglandine und Plättchenfunktion, H. K. Breddin. Schattauer Verlag. 1978, DAB 22. Tagung
  • Aoki N., Moroi M., Sakata Y., Yoshida N., Matsuda M. Abnormal plasminogen. A hereditary molecular abnormality found in a paitent with recurrent thrombosis. J. Clin. Invest 1978; 61: 1186–1195
  • Aoki N., Yamanaka T. The α2-plasmin inhibitor levels in liver diseases. Clin. Chim. Acta 1978; 84: 99–105
  • Aoki N., Saito H., Kamiya T., Koie K., Sakata Y., Kobakura M. Congenital deficiency of α2-plasmin inhibitor associated with severe hemorrhagic tendency. J. Clin. Invest 1979; 63: 877–884
  • Aoki N., Sabata Y., Matsuda M., Tateno K. Fibrinolytic states in a patient with congenital deficiency of α2-plasmin inhibitor. Blood 1980; 55: 483–488
  • Arnesen H., Rygh M., Ly B., Jakobsen E. Streptokinase resistance in medical patients in Olso. Scand. J. Haematol 1977; 18: 348–352
  • Arwin H., Um I., Claeson G., Ekenstam B. af, Aurell L. Thrombin activity measured with a new electric method. FEBS Lett 1976; 64: 95–97
  • åstedt B. No cross reaction between circulating plasminogen activator and urokinase. Thrombosis Res 1979; 14: 535–539
  • Auel H., Martin M. Die Technik des quantitativen Streptokinasenachweises im Plasma. Klin. Wschr 1975; 53: 809–814
  • Bael G., Kaufman J. M., Thiery M., Vermeulen A., Barbier F. Plasminogen, fibrinogen, α2-antiplasmin antithrombin-III levels during a single cycle of combined oral contraceptive regime. Acta Clinica Belgica 1981; 36: 280–285
  • Barlow G. H., Marder V. J. Plasma urokinase levels measured by chromogenic assay after infusions of tissue culture or urinary source material. Thrombosis Res 1980; 18: 431–437
  • Bee E. Org, Soberano M. E., Johnson A. J., Schoellmann G. Studies on the biochemistry of urokinase. Thrombosis & Haemostasis 1977; 38: 801–808
  • Bennett B., Ogston D. Role of complement, coagulation, fibrinolysis and kinins in normal haemostasis and disease. Haemostasis and Thrombosis, A. Bloom, D. P. Thomas. Churchill Livingstone. 1982; 236–251, Chapter 15
  • Bergquist D., Nilsson I. M. Heriditary alpha2-macroglobulin deficiency. Scand. J. Haematol 1979; 23: 433–436
  • Bergström K., Egberg N. Proteolytic activity in plasma using new chromogenic substrates. Abstract No. 577 of paper presented at the Vth Congress of the ISTH, Paris, 1975
  • Bernik M. B., Oller E. P. Increased plasminogen activator (Urokinase) in tissue culture after fibrin deposition. J. Clin. Invest 1973; 52: 823–834
  • Bigbee W. L., Weintraub H. B., Jensen R. H. Sensitive fluorescence assays for urokinase using synthetic peptide 4-methoxy-β-naphtylamide substrates. Analytical Biochemistry 1978; 88: 114–122
  • Binder B. R., Spragg J., Austen K. F. Purification and characterization of human vascular plasminogen activator derived from blood vessel perfusates. J. Biol. Chem 1979; 254: 1998–2003
  • Blasini R., Stemberger A., Wriedt-Lübbe I., Blümet G. Tissue proteases demonstrated by a histochemical method using chromogenic substrates. Thrombosis Res 1978; 13: 585–590
  • Blombäck M., Egberg N., Frisch P., Hellgren M., Mettinger K. L., Wahlberg T. Chromogenic peptide substrates in fibrinolysis. 186–195, In ref. 8
  • Blombäck M. Chromogenic substrates in the laboratory diagnosis of clotting disorders. Haemostasis and Thrombosis, A. L. Bloom, D. P. Thomas. Churchill Livingstone. 1981; 809–823
  • Borth W. A novel immunosorbent assay to characterize α2-macroglobulin proteinase complexes and the trypsin binding capacity of α2-M. Abstract 130 of the VIIIth Meeting of the FECTS. Aug., 1982
  • Bouma B. N., Miles L. A., Beretta G., Griffin J. H. Human plasma prekallikrein. Studies of its activation by activated factor XII and of its inactivation by diisopropyl phosphofluoridate. Biochemistry 1980; 19: 1151–1160
  • Bruhn H. D. On the significance of “anti-streptokinase” in streptokinase-induced thrombolytic therapy. Thrombosis Diathes. Haemorrh 1973; 30: 221–222, and Deutscher med. Wschr. 99, 1410–1411, 1974
  • Bruhn H. D., Albert J. P., Britz A., Brück M., Hartmann F., Niedermayer W. Plasma-Präkallikrein-Spiegel bei Hypertonie. Deutsche Med. Wschr 1982; 107: 797
  • Burnett D., Stockley R. A. Serum and sputum α2-macroglobulin in patients with chronic obstructive airways disease. Thorax 1981; 36: 512–516
  • Campbell J. A. The contact factors and their proteolytic interactions in hemostasis. Canad. J. Med. Tech 1980; 42: F20–F28
  • Campbell E. E., Shifman M. A., Lewis J. G., Pasqua J. J., Pizzo S. V. A colorimetric assay for releasable plasminogen activator. Clin. Chem 1982; 28: 1125–1128
  • Carlin G., Bang N. U., Saldeen T. Effect of dextran on plasma clot lysis. 331–333, In ref. 8
  • Castellino F. J. Recent advances in the chemistry of the fibrinolytic system. Chemical Reviews 1981; 81: 431–446
  • Cederholm-Williams S. A. Concentration of plasminogen and antiplasmin in plasma and serum. J. Clin. Pathol 1981; 34: 979–981
  • Cederholm-Williams S. A. The effect of streptokinase on the fibrin binding site of plasmin(ogen). Thrombosis Res 1981; 21: 649–654
  • Cederholm-Williams S. A., Spencer J. A.D., Wilkinson A. R. Plasma levels of selected haemostatic factors in new born babies. Thrombosis Res 1981; 23: 555–558
  • Cederholm-Williams S. A., De Cock F., Lijnen H. R., Collen D. Kinetics of the reactins between streptokinase, plasmin and α2-antiplasmin. Eur. J. Biochem 1979; 100: 125–132
  • Chesne S., Villiers C. L., Arlaud G. J., Lacroix M. B., Colomb M. G. Fluid-phase interaction of C1 inhibitor (C1-INH) and the subcomponents C1r and C1s of the first component of complement, C1. Biochem. J 1982; 201: 61–70
  • Chmielewska J., Kurecki T., Raczka E., Latallo Z. S. Plasminogen activator in various cells. 244–248, In ref. 8
  • Christensen U., Ipsen H. H. Steady-state kinetics of plasmin- and trypsin-catalysed hydrolysis of a number of tripeptide-p-nitroanilides. Biochimica Biophysica Acta 1979; 569: 177–183
  • Claeson G., Aurell L., Karlsson G., Friberger P. Substrate structure and activity relationships. 299–304, In ref. 2
  • Claeson G., Friberger P., Knös M., Eriksson E. Methods for determination of prekallikrein in plasma, glandular kallikrein and urokinase. Haemostasis 1978; 7: 76–78
  • Claeson G., Aurell L., Friberger P., Gustavsson S., Karlsson G. Designing of peptide substrates. Different approaches exemplified by new chromogenic substrates for kallikreins and urokinase. Haemostasis 1978; 7: 62–68
  • Claeson G., Aurell L., Karlsson G., Friberger P. Substrate structure and activity relationships. 37–48, In ref. 1
  • Claeson G., Aurell L. Small synthetic peptides with affinity for proteases in coagulation and fibrinolysis. 798–811, An overview. In ref. 9
  • Clemensen I. Different molecular forms of α2-antiplasmin. 131–136, In ref. 6
  • Clemensen I., Thorsen S., Müllertz S., Petersen L. C. Properties of the three different molecular forms of the α2-plasmin inhibitor. Eur. J. Biochem 1981; 120: 105–112
  • Cochrane C. G., Griffin J. H. Molecular assembly in the contact phase of the Hageman factor system. Am. J. Med 1979; 67: 657–668
  • Coleman P. L., Green G. D.J. A sensitive, coupled assay for plasminogen activator using a thiol ester substrate for plasmin. 616–626, In ref. 9
  • Collen D., Wiman B. Turnover of α2-antiplasmin and of the plasmin-α2-antiplasmin complex. 171–176, In ref. 6
  • Collen D., Edy J., Wiman B. Discrimination between antiplasmins: reaction mechanisms, biological role and assay of the fast-acting plasmin inhibitor in human plasma. 238–247, In ref. 5
  • Collen D. On the regulation and control of fibrinolysis. Thrombosis & Haemostasis 1980; 43: 77–89
  • Collen D., Stassen J.-M. Thrombolysis with human extrinsic (tissue-type) plasminogen activator in rabbits with experimental jugular vein thrombosis. Haemostasis 1982; 11(Suppl. 1)33
  • Colman R. W. Patho-physiology of the kallikrein system. Ann. Clin. Lab. Sci 1980; 10: 220–226
  • Colman R. W., Schapira M., Scott C. F. Regulation of the formation and inhibition of human plasma kallikrein. 261–270, In ref. 9
  • Cs-Szabó G., Pozsgay M., Elödi P. Investigation of the substrate-binding site of human plasmin using tripeptidyl-p-nitroanilide substrates. Thrombosis Res 1980; 20: 199–206
  • Cullman W., Dick W. A chromogenic assay for evaluation of α2-macroglobulin level in serum and cerebrospinal fluid. J. Clin. Chem. Clin. Biochem 1981; 19: 287–290
  • Cullman W., Dick W., Müller N. Verhalten des Heparin-Kofactors (Antithrombin III) bei Patienten mit Venenthrombose. Inn. Med 1981; 8: 235–238
  • Cullmann W., Körary P. M., Dick W., Czarnetzki B., Echternach-Hoppe K. A rapid method for functional determination of C1 esterase inhibitor in plasma. Clin. Chim. Acta 1982; 119: 237–242
  • Derkx F. H.M., Bouma B. N., Schalekamp M. P.A., Schalekamp M. A.D.H. An intrinsic factor XII-prekalli-krein-dependent pathway activates the human plasma renin-angiotensin system. Nature 1979; 280: 315–316
  • Dick W., Cullmann W., Müller N., Adler K. Factor XII assay with the chromogenic substrate Chromenzym PK. J. Clin. Chem. Clin. Biochem 1981; 19: 357–361
  • Drapier J. C., Teny J. P., Lemaire G., Petit J. F. Regulation of plasminogen activator secretion in mouse peritoneal macrophages. I. Role of serum studied by a new spectro-photometric assay for plasminogen activators. Biochimie 1979; 61: 463–471
  • Duckert F. Die chromogenen Substrate. Ihre diagnostische Anwendung in der Gerinnung und Fibrinolyse. Med. Labor 1979; 32: 25
  • Dudek-Wojciechowska G., Kopec M., Latallo Z. S. Inhibition of the fibrinolytic system by α2-macroglobulin. 312–315, In ref. 8
  • Edy J., De Cock F., Collen D. Inhibition of plasmin by normal and antiplasmin-depleted human plasma. Thrombosis Res 1976; 8: 513–518
  • Edy J., Collen D., Verstraete M. Quantitation of the plasma protease inhibitor antiplasmin with the chromogenic substrate S-2251. 315–322, In ref. 2
  • Egberg N., Bergström K. Studies on assays for plasma prekallikrein and for the monitoring of coumarol therapy. Haemostasis 1978; 7: 85–91
  • Egberg N., Bergström K. Synthetic chromogenic substrates in the assay for plasma prekallikrein and coagulation factors II and X. 61–70, In ref. 5
  • Egberg N., Gallimore M. J. Studies on Hageman factor, plasma prekallikrein, kallikrein “like” activity and kallikrein inhibition in plasma samples from normal subjects and clinical material. Plenum Press. 1982, Adv. Expt. Med. Biol., In press
  • Einarsson M., Forsberg B., Grafström E., Mattson C., Neiger K., Nilsson S., Uthne T. Effect on haemostasis of intravenous injection of α2-antiplasmin in cats treated with streptokinase, Submitted for publication
  • Eriksson E., Rosén S., Knös M., Friberger P. Chromogenic substrate methods for the determination of FVIIIC, endotoxin and plasminogen activator. Thrombosis & Haemostasis 1981; 46: 315
  • Eriksson E., Gyzander E., Teger-Nilsson A. C. Assay of tissue plasminogen activator utilizing plasminogen, poly-lysine and a chromogenic substrate. Haemostasis 1982; 11(Suppl. 1)89
  • Fareed J., Messmore H. L., Bermes E. W. New perspectives in coagulation testing. Clin. Chem 1980; 26: 1380–1391
  • Fink P. C., Lehr L., Urbaschek R. M., Kozak J. Limulus amebocyte lysate test for endotoemia. Investigations with a femtogram sensitive spectrophotometric assay. Klin. Wschr 1981; 59: 213–218
  • Friberger P., Knös M., Eriksson E. The use of chromogenic peptide substrates in fibrinolytic research and clinical practice. 212–218, In ref. 8
  • Friberger P., Axelsson G., Korsan-Bengtsen K. Determination of plasminogen by means of a chromogenic peptide substrate. Abstract of paper read at the Vth Int. Congr. Thrombosis and Haemostasis, Paris, 1975
  • Friberger P., Knös M., Gustavsson S., Aurell L., Claeson G. Methods for determination of plasmin, antiplasmin and plasminogen by means of substrate S-2251. Haemostasis 1978; 7: 138–145
  • Friberger P., Claeson G., Knös M., Aurell L., Arielly S., Simonsson R. Activity of plasminogen activators on tripeptide chromogenic substrates. 149–153, In ref. 3
  • Friberger P., Knös M. Functional assays of the components of the fibrinolytic system using a plasmin sensitive substrate. 73–92, A review. In ref. 7
  • Friberger P., Knös M., Mellstam L. A quantitative endotoxin assay utilizing LAL and a chromogenic substrate. Endotoxins and their detection with the limulus amebocyte lysate test, S. W. Watson, J. Levin, T. J. Novitsky. Alan R. Liss. 1982; 195–205
  • Friberger P., Aurell L., Claeson G. Chromogenic substrates for kallikreins and related enzymes. BirkhäuserAgents and Actions Supplements, H. Fritz, G. Dietze, F. Fiedler, G. L. Haberland, 1982; vol. 9: 83–90
  • Friedrich L., Hinterberger W., Thaler E., Lechner K. Die schnelle Plasmininhibitor (α2-Antiplasmin)-Aktivität bei Patienten nach Myocardinfarkt, chirurgischen Eingriffen und thrombotischen Ereignissen. Abstr. 143. 1. Kongress für Thrombose und Blutgerinnung. 1981; 87
  • Friedman R. B., Kwaan H. C., Szczecinksi M. Improved sensitivity of chromogenic substrate assays for urokinase and plasmin. Thrombosis Res 1977; 12: 37–46
  • Frisch E. P. Decreased α2-antiplasmin levels in patients suffering from obstructive peripheral arterial disease. Thrombosis Res 1980; 19: 701–703
  • Fujikawa K., Heimark R. L., Kurachi K., Davie E. W. Activation of bovine Factor XII (Hageman Factor) by plasma kallikrein. Biochemistry 1980; 19: 1322–1330
  • Fässler H., Walter M., Market G., Duckert F. The quantitative determination of urokinase with Chromozym UK. 249–250, In ref. 1
  • Fässler H., Duckert F., Marbet G. A. Assay with chromogenic substrates of in vivo activated proteases. Haemostasis 1978; 7: 158–163
  • Gaffney P. J., Philo R. D. Measurement of some haemostatic components using biological and amidolytic assays. 196–202, In ref. 8
  • Gallimore M. J., Aasen A. O., Lyngaas K. H.N., Larsbraaten M., Amundsen E. Falls in plasma levels of prekallikrein, high molecular weight kininogen, and kallikrein inhibitors during lethal endotoxin shock in dogs. Thrombosis Res 1978; 12: 307–318
  • Gallimore M. J., Aasen A. O., Amundsen E. Changes in plasma levels of prekallikrein, kallikrein, high molecular weight kininogen and kallikrein inhibitors during lethal endotoxin shock in dogs. Haemostasis 1978; 7: 79–84
  • Gallimore M. J., Fareid E., Stormorken H. The purification of a human plasma kallikrein with weak plasminogen activator activity. Thrombosis Res 1978; 12: 409–420
  • Gallimore M. J., Fareid E. Studies on human plasma inhibitors of plasmin, plasma kallikrein, trypsin, thrombin and urokinase, using chromogenic substrate assays. 248–261, In ref. 5
  • Gallimore M. J., Amundsen E., Aasen A. O., Larsbraaten M., Lyngaas K., Svendsen L. Studies on plasma antiplasmin activity using a new plasmin specific chromogenic tripeptide substrate. Thrombosis Res 1979; 14: 51–60
  • Gallimore M. J. Inhibitors of plasminogen activation present in human plasma. 199–217, In ref. 6
  • Gallimore M. J. Discrepancies between antigen concentrations and functional activities of plasma protease inhibitors. Protides of the Biological Fluids, H. Peeters. Pergamon Press. 1979; 345–348
  • Gallimore M. J., Aasen A. O., Smith-Erichsen N., Larsbraaten M., Lyngaas K., Amundsen E. Plasminogen concentrations and functional activities and concentrations of plasmin inhibitors in plasma samples from normal subjects and patients with septic shock. Thrombosis Res 1980; 18: 601–608
  • Gallimore M. J. Inhibition of the amidolytic activity of urokinase by human plasma. Thrombosis Res 1980; 17: 289–291
  • Gallimore M. J. Discrepancies between immunochemical levels and functional activities of plasma protease inhibitors. Abstract 5.02 of a paper held at the 28th annual colloquium on Protides of the Biological Fluids, Brussels, May, 51980
  • Gallimore M. J., Ford C. H.J., Howell A., Newman C. E. Further studies on components of the plasma kallikrein system in plasma samples from cancer patients and normal individuals. 256–258, In ref. 8
  • Gallimore M. J., Milford A. Ward. Studies on components of the plasma kallikrein and complement systems in plasma and serum samples from normal individuals and patients with hereditary angioedema. Plenum Press. 1982, In Adv. Expt. Med. Biol., In press
  • Gallimore M. J. Chromogenic substrate assays for studying components of the plasma kallikrein system in health and disease. Plenum Press. 1982, In Adv. Expt. Med. Biol., In press
  • Ganrot P. O. Determination of α2-macroglobulin as trypsin-protein esterase. Clin. Chim. Acta 1966; 14: 493–501
  • Gottlob R., Mattausch M., Porschinski K., Kramar R. The possible role of leucocytes in spontaneous and induced thrombolysis and some properties of leucocyte protease. 391–411, In ref. 2
  • Greineder D. K., Connorton K. J., David J. R. Plasminogen activator production by human monocytes. I. Enhancement by activated lymphocytes and lymphocyte products. J. Immunol 1979; 123: 2808
  • Griffin J. H. Role of surface in surface-dependent activation of Hageman factor (blood coagulation Factor XII). Proc. Natl. Acad. Sci. USA 1978; 75: 1998–2002
  • Günzler W. A., Steffens G. J., Ötting F., Buse G., Flohé L. Structural relationship between human high and low molecular mass urokinase. Hoppe-Seyler's Z. Physiol. Chem 1982; 363: 133–141
  • Gyzander E., Friberger P., Myrwold H., Noppa H., Olsson R., Teger-Nilsson A.-C., Wallmo L. Anti-plasmin determination by means of the plasmin specific substrate S-2251. Methodological studies and some clinical applications. 229–247, In ref. 1
  • Gyzander E., Teger-Nilsson A.-C. Activity of the α2-macroglobulin-plasmin complex on the plasmin specific substrate H-D-Val-Leu-Lys-p-nitroanilide. Thrombosis Res 1980; 19: 165–175
  • Gyzander E., Eriksson E., Teger-Nilsson A.-C. Determination of tissue plasminogen activator in plasma after adsorption on lysine-sepharose. Haemostasis 1982; 11(Suppl. 1)68
  • Harpel P. C. Plasmin inhibitor interactions. The effectiveness of α2-plasmin inhibitor in the presence of α2-macroglobulin. J. Exp. Med 1977; 146: 1033–1040
  • Hayashi S., Yamada K. Role of α2-plasmin inhibitor in the appearance of fibrinolytic activity during urokinase administration, and an evaluation of the optimal urokinase dosage. Thrombosis Res 1979; 16: 393–400
  • Hayashi S., Yamada K. Assay of urokinse activity in plasma with a chromogenic substrate. Thrombosis Res 1981; 22: 573–578
  • Heber H., Geiger R., Heimburger N. Human plasma kallikrein: Purification, enzyme characterization and quantitative determinaion in plasma. Hoppe-Seyler's Z. Physiol. Chem 1978; 359: 659–669
  • Hedner U., Nilsson I. M. Urokinase inhibitors in serum in a clinical series. Acta med. Scand 1971; 189: 185–189
  • Hedner U. Inhibitor(s) of plasminogen activation distinct from the other plasma protease inhibitors — a review. 189–197, In ref. 6
  • Heimburger N. Antithrombin III. Biochemische Wirkung. Kontrolle Antithrombotika. Hamburger Symposium Blutgerinnung 23rd., R. Marx, H. A. Thies. Roche, Basel 1981; 79–84
  • Hellgren M., Nygårds E. B. Blood coagulation and fibrinolysis in fertile women with thromboembolic complications and effects of venous occlusion. Thrombosis Res 1981; 24: 453–465
  • Hellgren M., Blombäck M. Studies on blood coagulation and fibrinolysis in pregnancy, during delivery and in the puerperium. Gynecol. Obstet. Invest 1981; 12: 141–154
  • Hemker H. C. Handbook of synthetic substrates for the coagulation and fibrinolytic system, In press
  • Hojima Y., Tankersley D. L., Miller-Andersson M., Pierce J. V., Pisano J. J. Enzymatic properties of human Hageman Factor fragment with plasma prekallikrein and synthetic substrates. Thrombosis Res 1980; 18: 417–430
  • Hoylaerts M., Rijken D. C., Lijnen H. R., Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J. Biol. Chem 1982; 257: 2912–2914
  • Huber K., Grasl B., Binder B. R. Plasminogenaktivatoraktivität und amidolytische Aktivität in Ratten-und Menschenharn. Abstract P 8.2 of a paper presented at the 2nd Congress of Thrombosis and Coagulation, Münster, Feb., 1982
  • Huseby R. M., Clavin S. A., Smith R. E., Hull R. N., Smithwick E. L. Studies on tissue culture plasminogen activator. II. The detection and assay of urokinase and plasminogen activator from LLC-PK1 cultures (porcine) by the synthetic substrate Nα-Benzyoloxycarbonyl-glycyl-glycyl-anginyl-4-methoxy-2-naphthylamide. Thrombosis Res 1977; 10: 679–687
  • Huseby R. M., Smith R. E. Synthetic oligopeptide substrates: Their diagnositc application in blood coagulation, fibrinolysis, and other pathologic states. Thrombosis and Hemostasis 1980; VI: 173–315, Seminars in
  • Ipsen H. H. Presteady state og steady state kinetiske undersøgelser af plasmin og trypsin katalysert hydrolyse af en raekke tripeptid-p-nitroanilider. Kemisk Laboratorium IV. København Universitet. juni, 1979, Rapport
  • Ipsen H. H., Christensen U. Kinetic studies of urokinase-catalysed hydrolysis of 5-oxo-L-prolylglycyl-L-anginine-4-nitroanilide. Biochimica Biophysica Acta 1980; 613: 476–481
  • Ito R., Statland B. E. Centrifuged analysis for plasma kallikrein activity, with use of the chromogenic substrate S-2302. Clin. Chem 1981; 27: 586–593
  • Ito R., Statland B. E., Solomon J., Fareed J., Bermes E. W., Walenga J., Perry J. F., Wehrly J. A. A clinical evaluation of an automated plasminogen assay. J. Clin. Chem. Clin. Biochem 1981; 19: 709
  • Iwanaga S., Kato H., Suga T., Ikari N., Hashimoto N., Fujii S. The kallikrein-kinin system: A functional role of plasma kallikrein and kininogen in blood coagulation. Biological Functions of Proteinases, H. Holzer, H. Tschesche. H. Springer-Verlag. 1979; 243–259
  • Jackson C. M., Christensen U. Collaborative assay of the KABI p-nitroanilide “standard”. Paper presented at the 1CTH meeting in London. StockholmSweden 1979, Available from KABI Diagnostica
  • Jacksson K. W., Esmon N., Tang J. Structural homology of streptokinase with serine proteases and possible relationships with staphylokinase. The Regulation of Coagulation, Mann, Taylor. Elsevier, North Holland Inc. 1980; 515–520
  • Jaffe J. P., Mosher D. F. Plasma antithrombin III and plasminogen levels in chronic plasmaphoresis. New Engl. J. Med 1981; 304: 789
  • Jespersen J., Knudsen L. H., Sidelmann J. The use of evacuated glass tubes for collection of blood samples for fibrinolytic assays. Thrombosis Res 1982; 25: 173–176
  • Jochum M., Witte J., Schiessler H., Selbmann H. K., Ruckdeschl G., Fritz H. Clotting and other plasma factors in experimental endotoxemia: Inhibition of degradation by exoneous proteinase inhibitors. Eur. surg. Res 1981; 13: 152–168
  • Kakkar V. V. Intermittent plasminogen-streptokinase treatment of deep vein thrombosis. 420–431, In ref. 8
  • Kalter E. S., Timmermans A., Bouma B. N. The kinin generating system during sepsis and bacterial shock. Agents and Actions Supplements, H. Fritz, G. Dietze, F. Fiedler, G. L. Haberland, Birkenhauser 1982; vol. 9: 638–644
  • Kasche V., Zöllner R. Tris(hydroxymethyl)methylamine is acylated when it reacts with acyl-chymotrypsin. Hoppe-Seyler's Physiol. Chem 1982; 363: 531–534
  • Kazama M., Tahara C., Sizuki Z., Gohchi K., Abe T. Abnormal plasminogen, a case of recurrent thrombosis. Thrombosis Res 1981; 21: 517–522
  • Keber D., Stegnar M. High degree of plasminogen activator stores depletion after venous occlusion and local exercise of arm. 350–353, In ref. 8
  • Klessen C., Stürzenbecker J., Markwardt F. Determination of factor XII in plasma using the kallikrein substrate Chromozym PK. Thrombosis Res 1982; 25: 501–505
  • Klingemann H.-G., Egbring R., Holst F., Gramse M., Havemann K. Digestion of α2-plasmin inhibitor by neutral proteases from human leucocytes. Thrombosis Res 1981; 24: 479–483
  • Kluft C., Jenks R. L., Astrup T. Production of plasminogen activator activity in factor XII-deficient plasma. Thrombosis Res 1977; 10: 759–764
  • Kluft C., Trumpi-Kolshoven M. M., Jie A. F.H. Crucial conditions for the determination of prekallikrein levels in plasma with chromogenic substrates. 84–92, In Ref. No. 5
  • Kluft C. Determination of prekallikrein in human plasma: optimal conditions for activating prekallikrein. J. Lab. Clin. Med 1978; 91: 83–95
  • Kluft C., Vellenga E., Brommer E. J.P. Homozygous α2-antiplasmin deficiency. The. Lancet July 28, 1979; 206
  • Knös M., Friberger P. Methods for plasminogen determination in human plasma and for streptokinase standardization. 154–158, In ref. 3
  • Koie K., Kamiya T., Ogata K., Takamatsu J. α2-plasmin-inhibitor deficiency (Miyasato disease). The Lancet Dec. 23&30, 1978; 1334–1336
  • Kruithof E. K.O., Ransijn A., Bachmann F. Inhibition of tissue plasminogen activator (TA) by human plasma. Haemostasis 1982; 11(Suppl. 1)60
  • Kopeć M., Kaczanawska J., Stachurska J., Tomaczak Z., Wojtecka-Lukasik E., Boykowska K., Lopaciuk S. Effect of granulocytic neutral proteases on some clotting factors. 75–77, In Ref. 8
  • Larsson R. L., Olsson P. I. Mode of establishing the presence of proteolytic enzymes. Swedish patent application. 7907013–2
  • Latallo Z. S., Kowalska-Loth B., Chmielewska J., Teisseyre E., Raczka E., Kopec M. A new approach to study factors from tumour cells which influence the clotting and fibrinolytic systems. 411–415, In ref. 8
  • Latallo Z. S. Chromogenic substrate. Chapter 11. Recent Advances in Blood Coagulation. Churchill Livingstone. 1981; Vol. 3
  • Latallo Z. S., Teisseyre E. Preliminary experience with a new chromogenic substrate in studies on blood coagulation and fibrinolysis. Abstract f3a6 of a paper presented at the 9th FEBS Meeting. Budapest 1974
  • Latallo Z. S., Teisseyre E., Lopacink S. Evaluation of a fibrinolytic profile of plasma using chromogenic substrates. 262–268, In ref. 5
  • Latallo Z. S., Teisseyre E., Lopacink S. Assessment of plasma fibrinolytic system with use of chromogenic substrate. Haemostasis 1978; 7: 150–154
  • Latallo Z. S. 139, Discussion in ref. 5
  • Latallo Z. S., Teisseyre E., Raczka E. Activators of plasminogen, measurement using chromogenic substrates. 154–164, In ref. 5
  • Latallo Z. S., Uchman B., Rymaszcwski Z., Berent H., Teisseyre E., Palester-Chlebowczyk M. Chromogenic substrates in monitoring urokinase therapy. 203–207, In ref. 8
  • Lawson D. E., Mitchell G. A., Huseby R. M. A sensitive fluorescent assay for determining α2-plasmin inhibitor using a synthetic substrate. Thrombosis Res 1979; 14: 323–332
  • Lehmann D., Lill H., Schaich E., Grassl M. The dependence of the molar absorptivity of 4-nitroaniline, 3-carboxy-4-nitroaniline and 4-nitrophenol on the reaction conditions. Enzymes in Health and Disease. 1978; 107–114, Inaug. Scient. Meet. Int. Soc. Clin. Enzymol. London, 1977. Kager
  • Lewis D. H., Bengtsson M.-B., Liljedahl S.-O., Larsson J. The use of chromogenic substrates for the determination of kallikrein and other serine proteases in plasma and synovial fluid in man. Advances in Biosciences. Vol. 17. Current Concepts in Kinin Research, H. Haberland, U. Hamberg. Pergamon Press. 1979
  • Lijnen H. R., Jacobs G., Collen D. Histidine-rich glycoprotein in a normal and a clinical population. Thrombosis Res 1981; 22: 519–523
  • Lottenberg R., Jackson C. M. Solution composition dependent variation in extinction coefficients for p-nitroaniline, Submitted for publication
  • Lottenberg R., Christensen U., Jackson C. M., Coleman P. L. Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates. Proteolytic Enzymes. Methods in Enzymology, L. Lorand. Academic Press. 1981; vol. 80: 341–364
  • Lämmle B., Eichlisberger R., Marbet G. A., Duckert F. Amidolytic activity in normal human plasma assessed with chromogenic substrates. Thrombosis Res 1979; 16: 245–254
  • Lämmle B., Duckert F. Different assessment of plasmin with different substrates. In vitro alteration of plasmin, influence of epsilon-aminocaproic acid and tranexamic acid upon its activity. Thrombosis Haemostasis 1980; 43: 112–117
  • Lämmle B., Duckert F. Plasma prekallikrein determinations. New Engl. J. Med 1982; 306: 613
  • Mahour G. H., Song M. K., Adham N. F., Rinderknecht H. Alpha2-macroglobulin deficiency in a patient with Ehlers Danlos syndrome. Pediatrics 1978; 61: 894–897
  • Matsuda M., Wakabayashi K., Aoki N., Morioka Y. α2-Plasmin inhibitor is among acute phase reactants. Thrombosis Res 1980; 17: 527–532
  • Marbet G. A., Gattlen D., Duckert F. Thrombolysis with porcine plasmin followed by low dose urokinase in deep leg vein thrombosis (DVT). Haemostasis 1982; 11(Suppl. 1)27
  • Matsuo O., Kosugi T., Mihara H., Ohki Y., Matsuo T. α2-plasmin inhibitor levels in relation to modes of urokinase administration. Thrombosis Res 1980; 19: 271–275
  • Mattler L. E., Bang N. U. Serine protease specificity for peptide chromogenic substrates. Thrombosis Haemostasis 1977; 38: 776–792
  • Mattsson C., Nyberg-Arrhenius V., Wallén P. Dissolution of thrombi by tissue plasminogen activator, urokinase and streptokinase in an artificial circulating system. Thrombosis Res 1981; 21: 535–545
  • McClintock D. K., Englert M. E., Dziobkowski C., Snedeker E. H., Bell P. H. Two distinct pathways of the streptokinase-mediated activation of highly purified human plasminogen. Biochemistry 1974; 13: 5334–5344
  • Meneghini P., Intra E., Poggio R. On the mechanism of the indirect thrombolytic therapy. 297–299, In ref. 8
  • Mettinger K. L., Egberg N. A study of hemostasis in ischemic cerebrovascular disease. III. Abnormalities in vascular plasminogen activators, antiactivators and α2-antiplasmin. Thrombosis Res 1982; 26: 203–210
  • Miles L. A., Burnier J. P., Verlander M. S., Goodman M., Kleiss A. J., Griffin J. H. Inactivation of purified human α2-antiplasmin and purified human C1 inhibitor by synthetic fibrinolytic agents. Blood 1981; 57: 1015–1024
  • Mussoni L., Raczka E., Chmielewska J., Donati M. B., Latallo Z. S. Plasminogen assay in rabbits, rat and mouse plasma using the chromogenic substrate S-2251. Thrombosis Res 1979; 15: 341–349
  • Mussoni L., Coen D., Balconi G., Delaini F., Donati M. B. Plasminogen activator activity of cells from primary and metastases of the Lewis lung carcinoma. 85–89, In ref. 8
  • Müllertz S. The primary plasmin-inhibitor, α2-plasmin-inhibitor or α2-antiplasmin. 87–101, A review. In ref. 6
  • Nagamatsu A., Soeda S. Effects of human granulocyte elastase in fibrinolysis. Chem. Pharm. Bull 1981; 29: 1121–1129
  • Nagase H., Cawston T. E., DaSilva M., Barrett A. J. Identification of plasma kallikrein as an activator of latent collagenase in rheumatoid synovial fluid. Biochim. Biophys. Acta 1982; 702: 133–142
  • Naito K., Aoki N. Assay of α2-plasmin inhibitor activity by means of a plasmin specific tripeptide substrate. Thrombosis Res 1978; 12: 1147–1156
  • Nieuwenhuizen W., Wijngaards G., Groeneveld E. Fluorogenic substrates for sensitive and differential estimation of urokinase and tissue plasminogen activator. Haemostasis 1978; 7: 146–149
  • Nigretto J. M., Jozefowicz M. Electrochemical activity determination of trypsin-like enzymes. I. Trypsin. Thrombosis Res 1980; 17: 611–622
  • Nilsson T., Cedergren B., Wiman B. On the significance of the two forms of human α2-antiplasmin with different affinity for the lysine-binding sites in plasminogen. Haemostasis 1982; 11(Suppl. 1)62
  • Nolan C., Hall L. S., Barlow G. H., Tribby I. E. Plasminogen activator from human embryonic kidney cell cultures. Evidence for a proactivator. Biochim. Biophys. Acta 1977; 496: 384–400
  • Norman P. S., Hill B. M. Studies of the plasmin system. III. Physical properties of the two plasmin inhibitors in plasma. J. Exp. Med 1958; 108: 639–649
  • Oh-Ishi S., Katori M. Fluorometric assay for plasma prekallikrein using peptidylmethyl-coumarinyl-amide as a substrate. Thrombosis Res 1979; 14: 551–559
  • Ohki M., Nakamura T., Morita T., Iwanaga S. A new endotoxin sensitive factor associated with hemolymph coagulation system of horseshoe crab (Limulidae). FEBS Letters 1980; 120: 217–220
  • Oka K., Tanaka K. Histochemical demonstration of thrombin using fluorogenic substrate. Thrombosis Res 1980; 19: 125–128
  • Okamoto U., Horie N., Nagamatsu Y., Yamamoto J.-I. Plasminogen-activator in human early milk: Its partial purification and characterization. Thrombosis Haemostasis 1981; 45: 121–126
  • Orenstein N. S., Dvorak H. F., Blanchard M. H., Young M. Nerve growth factor: A protease that can activate plasminogen. Proc. Natl. Acad. Sci. USA 1978; 75: 5497–5500
  • Paar D., Maruhn D. Spectrophotometric determination of urokinase in urine after gel filtration, using the chromogenic substrate S-2444. J. Clin. Chem. Clin. Biochem 1980; 18: 557–562
  • Perry J. F., Wehrly J. A., Siefring G. E., Jr., Ito R., Stratland B. E., Walenga J., Kelly J., Fareed J. Development and clinical efficacy of a fully automated assay for plasminogen on the DuPont “aca” discrete clinical analyzer. Haemostasis 1982; 11(Suppl. 1)69
  • Petersen L. C., Clemmensen I. Kinetics of plasmin inhibition in the presence of a synthetic tripeptide substrate. The reaction with pancreatic trypsin inhibitor and two forms of α2-plasmin inhibitor. Biochem. J 1981; 199: 121–127
  • Philo R. D., Gaffney P. J. Assay methodology for urokinase: Its use in assessing the composition of mixtures of high- and low-molecular weight urokinase. Thrombosis Res 1981; 21: 81–88
  • Philo R. D., Gaffney P. J. Plasmin potency estimates: Influence of the substrate used in assay. Thrombosis Haemostasis 1981; 45: 107–109
  • Philo R. D., Gaffney P. J. Some observations on the assay of plasminogen using streptokinase and S-2251. Haemostasis 1982; 11(Suppl. 1)66
  • Plow E. F., Edgington T. S. An alternative pathway for fibrinolysis. 1. The cleavage of fibrinogen by leucocyte proteases of physiologic pH. J. Clin. Invest 1975; 56: 30–38
  • Plow E. F. The major fibrinolytic proteases of human leucocytes. Biochim. Biophys. Acta 1980; 630: 47–56
  • Plow E. F., Plescia J. Non-plasmin mediated fibrinolysis. 70–74, In ref. 8
  • Pochron S. P., Mitchell G. A., Albareda I., Huseby R. M., Gargiulo R. J. A fluorescent substrate assay for plasminogen. Thrombosis Res 1978; 13: 733–739
  • Raczka E., Quintana A., Chmielewska J., Latallo Z. S. Changes in fibrinolytic and clotting system in tumour bearing mice. 248–253, In ref. 8
  • Ragni M. V., Lewis J. H., Hasika U., Spero J. A. Prekallikrein (Fletcher factor) deficiency in clinical disease states. Thrombosis Res 1980; 18: 45–54
  • Ratnoff O. D., Saito H. Evidence that Fitzgerald factor counteracts inhibition by kaolin or ellagic acid of the amidolytic properties of a plasma kallikrein. Blood 1976; 47: 243–251
  • Ratnoff O. D., Saito H. Interactions among Hageman factor, plasma prekallikrein, high molecular weight kininogen, and plasma thromboplastin antecedent. Proc. Natl. Acad. Sci. USA 1979; 76: 958–961
  • Ratnoff O. D., Saito H. Amidolytic properties of single-chain activated Hageman factor. Proc. Natl. Acad. Sci. USA 1979; 76: 1461–1463
  • Ratnoff O. D. Studies on the inhibition of ellagic acid-activated Hageman factor (Factor XII) and Hageman Factor Fragments. Blood 1981; 57: 55–58
  • Ratnoff O. D., Gordon E. M., Douglas J. G. Some recent advances in surface-mediated reactions. Abstract PL-3–5 in the International Congress ISH-ISBT. Aug., 1982
  • Reddy K. N.N. Mechanism of activation of human plasminogen by streptokinase. Fibrinolysis, Reddy, Kline. CRC Monograph, 1981; 71–94
  • Reddy K. N.N., Wagner C. J. Studies on the stability of plasmin. 374–380, In ref. 8
  • Rijken D. C., Wijngaards G., Welbergen J. Relationship between tissue plasminogen activator and the activators in blood and vascular wall. Thrombosis Res 1980; 18: 815–830
  • Rijken D. C., Collen D. Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J. Biol. Chem 1981; 256: 7035–7041
  • Rijken D. C., Hoylaerts M., Collen D. Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator. J. Biol. Chem 1982; 257: 2920–2925
  • Robbins K. C., Markus G. The interaction of human plasminogen with streptokinase. Fibrinolysis: Current Fundamental and Clinical Concept, P. J. Gaffney, S. Balkurulatins. Academic Press. 1978; 61–75
  • Robbins K. C. The regulation and control of the blood fibrinolytic system. 3–13, In ref. 8
  • Robbins K. C., Wohl R. C., Summaria L. Plasminogen chemistry and activation. 110–113, In ref. 8
  • Robbins K. C., Wohl R. C., Summaria L. Plasmin and plasminogen activators: Kinetics and kinetics of plasminogen activation. 588–591, In ref. 9
  • Róka L. Einsatz von chromogenen Substraten in der Gerinnungsanalyse. Medizintechnik 1979; 26: 139
  • Róka L., Rasche H. Blutgerinnungsdiagnostik mit chromogenen Substraten. Internist 1980; 21: 189–194
  • Rumpf K. W., Becker K., Kreusch U., Schmidt S., Vetter R., Scheler F. Evidence for a role of plasma kallikrein in the activation of prorenin. Nature 1980; 283: 482–483
  • Rånby M., Wallén P. A sensitive parabolic rate assay for the tissue plasminogen activator. 233–235, In ref. 8
  • Saito H., Goodnough L. T., Soria J., Soria C., Aznar J., España F. Heterogeneity of human prekallikrein deficiency (Flether trait). Evidence that five of 18 cases are positive for cross-reacting material. N. Engl. J. Med 1981; 305: 910–914
  • Saito H. The participation of plasma thromboplastin antecedent (factor XI) in contact-activated fibrinolysis. Proc. Soc. Exper. Biol. Med 1980; 164: 153–157
  • Sakata Y., Aoki N. Molecular abnormality of plasminogen. J. Biol. Chem 1980; 255: 5442–5447
  • Samama M., Schlegel N., Cazanave B., Horellou M. H., Conard J., Castel M., Donenias R. α2-antiplasmin assay: Amidolytic and immunological method. Critical evaluation. Results in a clinical material. 93–101, In ref. 7
  • Samama M., Schlegel N., Castel M., Cazenave B., Horellou M. H., Douenias R. Biological and immunological studies of plasminogen activation in vitro by urokinase (UK I and UK II). 369–374, In ref. 8
  • Sandberg H., Gellerbring A.-K., Andersson L.-O. Determination of platelet factor 3 in whole blood by a chromogenic peptide substrate assay. Thrombosis Res 1980; 18: 871–882
  • Saugstad O. D., Aasen A. O., Guldvog I., Lium B., Larsbraaten M., Lyngaas K., Amundsen E. Activation of plasma kallikrein-kinin and fibrinolytic systems during experimental lung insufficiency in dogs. Microvascular Res 1979; 18: 290
  • Sayama S., Kashiwagi H., Ogawa T., Terada K., Soma H., Kato M. Circulating levels of prekallikrein and kallikrein in pregnancy and labor. Biological Research in Pregnancy 1981; 2: 90–94
  • Schapira M., Scott C. F., Colman R. W. Protection of human palsma kallikrein from inactivation by C1 inhibitor and other protease inhibitors. The role of high molecular weight kininogen. Biochemistry 1981; 20: 2738–2743
  • Schapira M., Scott C. F., Colman R. W. Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma. J. Clin. Invest 1982; 69: 462–468
  • Schapira M., Silver L. D., Scott C. F., Colman R. W. New and rapid functional assay for C1-inhibitor in human plasma. Blood
  • Schramm W., Penker W., Rupp P., Philapitsch A. Hypercoaguability. Diagnostic value of C1-INA. Abstract F-167 of the International Congress ISH-ISBT. Aug., 1982
  • Schapira M., Silver L. D., Scott C. F., Colman R. W. New and rapid functional assay for C1-inhibitor in human plasma. Blood
  • Scott C. F., Liu C. Y., Colman R. W. Human plasma prekallikrein: a rapid high-yield method for purification. Eur. J. Biochem 1979; 100: 77–83
  • Scott C. F., Colman R. W. Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma. J. Clin. Invest 1980; 65: 413–421
  • Scott C. F., Kirby E. P., Schick P. K., Colman R. W. Effect of surfaces on fluid-phase prekallikrein activation. Blood 1981; 57: 553–560
  • Scully M. F., Kakkar V. V. Measurement of degraded forms of plasminogen in human plasma. Thrombosis Res 1980; 17: 345–352
  • Scully M. F., Newman S. E., Clark S. E., Kakkar V. V. Evaluation of a chromogenic mehtod for endotoxin measurement. Thrombosis Res 1980; 20: 263–270
  • Shakespeare M., Wolf P. The demonstration of urokinase antigen in whole blood. Thrombosis Res 1979; 14: 825–835
  • Shimada H., Mori T., Takada A., Takada Y., Noda Y., Takai I., Kohda H., Nishimura T. Use of chromogenic substrate S-2251 for determination of plasminogen activator in rat ovaries. Thrombosis Haemostasis 1981; 46: 507–510
  • Silverberg M., Dunn J. T., Garen L., Kaplan A. P. Autoactivation of human Hageman factor. Demonstration utilizing a synthetic substrate. J. Biol. Chem 1980; 255: 7281–7286
  • Simonsson R., Arielly S., Friberger P., Aurell L. Chromogenic substrates for granulocyte elastase, chymotrypsin and the subcomponents of C1-esterase. Thrombosis Haemostasis 1981; 46: 313
  • Smith R. A.G. Acyl-enzymes as fibrinolytic pro-drugs. Haemostasis 1982; 11(Suppl. 1)33
  • Snape T. J., Griffith D., Vallet L., Wesley E. D. The assay of prekallikrein activator in human blood products. Develop. Biol. Standard 1979; 44: 115–120
  • Soria J., Soria C., Samama M. Dosage du plasminogine à l'aide d'un substrat chromogine tripeptidique. Path. Biol 1976; 24: 725–729
  • Soria J., Soria C., Samama M. A plasminogen assay using a chromogenic synthetic substrate: Results from clinical work and from studies of thrombolysis. 337–346, In ref. 2
  • Soria J., Soria C., Bertrand O., Lefur M. A., Drowet L., Baudony Y., Dupuy E., Tabelem G., Caen J. Congenital abnormal plasminogen: Plasminogen Paris 1-relationship with thrombosis. Haemostasis 1982; 11(Suppl. 1)1
  • Soria J., Soria C., Bertrand C., Dunn F., Samama M., Bachmann F. The amidolytic activity of the SK-plasminogen complex is enhanced by a potentiator which is generated in the presence of vascular plasminogen activator — role of fibrin degradation products. Thromb. Haemostasis 1982; 47: 193–196
  • Sottrup-Jensen L., Petersen T. E., Magnusson S. In. Atlas of protein sequence and structure 1978; 5(suppl. 3)91
  • Sottrup-Jensen L., Petersen T. E., Magnusson S. Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate that can react rapidly to incorporate not only methyl-amine or putrescine but also proteins lacking proteinase activity. FEBS Letters 1981; 128: 123–126
  • Soulier J. P., Gozin D. Assay of Fletcher factor (plasma prekallikrein) using an artificial clotting reagent and a modified chromogenic assay. Thrombosis Haemostasis 1979; 42: 538–547
  • Steinbuch M., Lambin P., Granier C., Kichenin V., Garnier A. Inactivation of alpha2-macroglobulin by aliphatic amines. 281–290, In ref. 6
  • Stenbjerg S. Inherited alpha2-macroglobulin deficinecy. Thrombosis Res 1981; 22: 491–495
  • Sterrenberg L., Brommer E. J.P., Haak H. L. Evidence of fibrinogen breakdown by leukocyte enzymes in a patient with acute pormyelocytic leukaemia. Br. J. Haematology
  • Stormorken H., Ritland S., Baklund A. Plasminogen, prekallikrein and antithrombin III in liver disease as assayed with synthetic chromogenic substrates. Proceedings of ad hoc Discussion Group on Synthetic Substrates and Inhibitors of Coagulation and Fibrinolysis, ICTH XXII Annual Meeting. Kyoto 1976
  • Stormorken H. A new era in the laboratory evaluation of coagulation and fibrinolysis. Thrombosis Haemostasis 1976; 36: 299–301
  • Stormorken H. Activation and interaction of some defence system. Recent Advances in Blood Coagulation 1977; 2: 35–58, Chapter 2
  • Stormorken H., Baklund A., Gallimore M., Ritland S. Chromogenic substrate assay of plasma prekallikrein. With a note on its site of biosynthesis. Haemostasis 1978; 7: 69–75
  • Strickland D. K., Morris J. P., Castellino F. J. Enhancement of the streptokinase-catalyzed activation of human plasminogen by human fibrinogen and its plasminolysis products. Biochemistry 1982; 21: 721–728
  • Suenson E., Thorsen S. Secondary-site binding of Glu-plasmin, Lys-plasmin and miniplasmin to fibrin. Biochem. J 1981; 197: 619–628
  • Sundsmo J. S., Wood L. M. Activated factor B (Bb) of the alternative pathway of complement activatior cleaves and activates plasminogen. J. Immunol 1981; 127: 877–880
  • Takada A., Takada Y. Stuies on SK-potentiator of plasminogen in human plasma. Thrombosis Res 1978; 13: 325–385
  • Takada A., Ohashi H., Matsuda H., Takada Y. Effects of tranexamic acid, cis-AMCHA, and ϵ-amino hexanoic acid on the activation rate of plasminogen by urokinase in the presence of clot. Thrombosis Res 1979; 14: 915–923
  • Takada A., Unmo T., Takada Y. Influence of coagulation on the activation of plasminogen by strepto kinase and urokinase. Thrombosis Haemostasis 1979; 42: 901–908
  • Takada Y., Takada A. Influence of dextran sulfate and tranexamic acid on the activation of plasminogen by urokinase. Thrombosis Res 1979; 10: 865–869
  • Takada A., Takada Y. Hydrolysis of chromogenic substrates and TAME by the mixture of α2-macro-globulin and trypsin. Thrombosis Res 1980; 18: 205–211
  • Takada A., Takada Y. Interaction of plasmin with α2-macroglobulin and α2-antiplasmin in the presence and absence of tranexamic acid. Thrombosis Res 1980; 18: 237–240
  • Takada A., Mochizuki K., Takada Y. Further characterization of SK-potentiators of plasminogen. Thrombosis Res 1980; 19: 485–492
  • Takada A., Mochizuki K., Takada Y. Effects of SK-potentiator and fibrinogen on SK-plasminogen complex in the presence of tranexamic acid. Thrombosis Res 1980; 19: 767–773
  • Takada A., Takada Y. Enzymatic protperties of plasmins converted from acid-treated and native Glu-and Lys-plasminogens by urokinase. Thrombosis Res 1981; 21: 593–601
  • Takada A., Takada Y. Conversion of Glu-plasminogen to plasmin by urokinase in the presence of tranexamic acid. Thrombosis Res 1981; 22: 437–443
  • Takada A., Takada Y. Activation of Glu-plasminogen by urokinase in the presence of fibrinogen, fibrin, and SK-potentiator. Thrombosis Res 1981; 22: 497–501
  • Takada A., Takada Y. Conversion of proteolytically modified form (Lys-form) of human plasminogen to plasmin by urokinase in the presence of tranexamic acid. Thrombosis Res 1981; 23: 411–419
  • Tankersley D. L., Fournel M. A., Schroeder D. D. Kinetics of activation of prekallikrein by prekallikrein activator. Biochemistry 1980; 19: 3121–3127
  • Teger-Nilsson A.-C., Eriksson E., Gyzander E., Medegård A., Risberg B. Bestimmung der Fibrinolyse mit chromogenen Peptidsubstraten. Folia Haematol. (Leipzig) 1982; 109: 121–134
  • Teger-Nilsson A.-C., Friberger P., Gyzander E. Antiplasmin determination by means of a chromogenic tripeptide substrate. 305–313, In ref. 2
  • Teger-Nilsson A.-C., Gyzander E., Myrwold H., Noppa H., Olsson R., Wallmo L. Determination of fast-acting plasmin inhibitor (α2-antiplasmin) in plasma from patients with tendency to thrombosis and increased fibrinolysis. Haemostasis 1978; 7: 155–157
  • Thomas L. L.M., Sturk A., Kahlé L. H., ten Cate J. W. Quantitative endotoxin determination in blood with a chromogenic substrate. Clin. Chim. Acta 1981; 116: 63–68
  • Thomas L. L.M., Buller H. R., Sturk A., ten Cate J. W. Quantitative endotoxin determination in blood with a chromogenic substrate. Relation with antithrombin-III (AT-III), plasminogen (Plg) and septicemia. Brit. J. Haematol 1982; 50: 689
  • Thomas L. L.M., Henny C. P., Büller H. R., Sturk A., Joop K., ten Cate J. W. Chromogenic endotoxin determination in blood — clinical relevance. Klin. Wschr 1982; 60: 759–760
  • Toki N., Sumi H., Sasaki K., Robbins K. C. Oral administration of high molecular weight urokinase in human subjects and in an experimental dog model. 439–440, In ref. 8
  • Toki N., Tahasugi S., Ishizu K., Sato H., Sumi H. Studies on the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase. Thrombosis Haemostasis 1982; 47: 8–13
  • Tölö H., Suomela H. An optimized assay for prekallikrein activator activity in human plasma products. Thrombosis Res 1982; 27: 35–44
  • Triplett D. A. New methods in coagulation XIV-XVI. CRC Critical Reviews in Clinical Laboratory Sciences. 1981; 57–84
  • Van Leuven F., Cassiman J.-J., Van den Berghe H. Functional modificatons of α2-macroglobulin by primary amines. II. Inhibition of covalent binding of trypsin to α2-M by methylamine and other primary amines. J. Biol. Chem 1981; 256: 9023–9027
  • van Vliet A. C.M., van Vliet H. H.D.M., Dzoljić-Danilović G., Wilson J. H.P. Plasma prekallikrein and endotoxemia in liver cirrhosis. Thrombosis Haemostasis 1981; 45: 65–67
  • van Vliet H. H.D.M. Experiences with the determination of kallikrein, plasminogen and antiplasmin using chromogenic substrate: Clinical application. 103–112, In ref. 8
  • Velasco F., Torres A., Andres P., Duran M. I. Functional activities and concentrations of plasmin inhibitors in normal subjects and DIC patients. Thromb. Haemostasis 1982; 47: 275–277
  • Verheijen J. H., Mullaart E., Chang G., Kluft C. A sensitive spectrophotometric assay for tissue type plasminogen activator. Haemostasis 1982; 11(Suppl. 1)67
  • Venneröd A. M., Laake K. Prekallikrein and plasminogen proactivator: absence of plasminogen proactivator in Fletcher factor deficient plasma. Thrombosis Res 1976; 8: 519–522
  • Verstraete M., Vermylen J., Amery A., Vermylen C. Thrombolytic therapy with streptokinase using a standard dosage scheme. Brit. Med. J 1966; 5485: 454–456
  • Vinazzer H. Assay of total factor XII and of activated factor XII in plasma with a chromogenic substrate. Thrombosis Res 1979; 14: 155–166
  • Walker I. D., Gallimore M. J., Imrie C. W., Davidson J. F. The coagulation, fibrinolytic and plasma kallikrein systems in acute pancreatitis. 291–293, In ref. 8
  • Walker J. E., Campbell D. M., Ogston D. Inhibitors of fibrinolysis in amniotic fluid. Thrombosis Haemostasis?/ 1980; 32–34
  • Wallén P., Råby M., Bergsdorf N., Kok P. Purification and characterization of tissue plasminogen activator: on the occurrence of two different forms and their enzymatic properties. 16–23, In ref. 8
  • Whur P., Magudia M., Boston J., Lockwood J., Williams D. C. Plasminogen activator in cultured Lewis lung carcinoma cells measured by chromogenic substrate assay. Br. J. Cancer 1980; 42: 305–314
  • Wiggins R. C., Bouma B. N., Cochrane C. G., Griffin J. H. Role of high-molecular-weight kininogen in surface-binding and activation of coagulation Factor XI and prekallikrein. Proc. Natl. Acad. Sci. USA 1977; 74: 4636–4640
  • Wijngaards G., Nieuwenhuizen W. Fluorogenic substrates and the assay of urokinase and tissue plasminogen activator. 123–131, In ref. 7
  • Wijngaards G., Groeneveld E. Inhibition of fibrinolytic enzymes by patient plasmas tested by different methods. 328–331, In ref. 8
  • Wijngaards G., Kluft C., Groeneveld E. Demonstration of urokinase-related fibrinolytic activity in human plasma. Brit. J. Haematol 1982; 51: 165–169
  • Wiman B. On the reaction of plasmin and plasmin-streptokinase complex with aprotinin or α2-antiplasmin. Thrombosis Res 1980; 17: 143–152
  • Wiman B., Collen D. On the mechanism of the reaction between plasmin and α2-antiplasmin. Kinetic and structural changes. 145–156, In ref. 6
  • Wiman B., Nilsson T. A new simple method for determination of C1-esterase inhibitor activity in plasma. Clin. Chim. Acta
  • Wiman B., Mellbring G., Rånby M. Plasminogen activator release during venous stasis and exercise as determined by a new specific assay. Clin. Chim. Acta
  • Witt I., Svendsen L., Koeppen H., Hasler K. Bestimmung von Plasma-kallikrein mit einem chromogenen Peptid-Substrat: Methodik und klinische Anwendung. Fresenius Z. Anal. Chem 1978; 290: 104–105
  • Witt I., Tritschler W., Bablok W. α2-Macroglobulin: Reference values in serum and plasma with a chromogenic substrate (Chromozym TRY). J. Clin. Chem. Clin. Biochem 1981; 19: 877–878
  • Wohl R. C., Summaria L., Robbins K. C. Physiological activation of the human fibrinolytic system. Isolation and characterization of human plasminogen variants. Chicago I and Chicago II. J. Biol. Chem 1979; 254: 9063–9069
  • Wohl R. C., Summaria L., Robbins K. C. Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37d`C. J. Biol. Chem 1980; 255: 2005–2013
  • Wun T.-C., Schleuning W. D., Reich E. Isolation and characterization of urokinase from human plasma. J. Biol. Chem 1982; 257: 3276–3283
  • Yokoyama T., Uchida K., Niinobe M., Fujii S. Effects of two polyethylenglycol flufenamates on fibrinolytic enzymes. Japan J. Biol. Chem 1981; 10: 47–51

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