Synthetic Peptide Substrates in Hemostatic Testing

References

• Suttie J. W., Jackson C. M. Prothrombin structure, activation and biosynthesis. Physiol. Rev. 1977; 57(1)1
   PubMed Web of Science ®Google Scholar
• Jackson C. M., Nemerson Y. Blood coagulation. Ann. Rev. Biochem. 1980; 49: 765
   PubMed Web of Science ®Google Scholar
• Davie E. W., Fujikawa K. Basic mechanism in blood coagulation. Ann. Rev. Biochem. 1975; 44: 799
   PubMed Web of Science ®Google Scholar
• Baugh R. F., Hougie C. The chemistry of blood coagulation. Clin. Hematol. 1979; 8(1)3
   PubMedGoogle Scholar
• Davie E. W., Fujikawa K., Kurachi K., Kisiel W. The role of serine proteases in the blood coagulation cascade. Adv. Enzymol. 1979; 49: 277
   Google Scholar
• Troll W., Sherry S., Wachman J. The activation of thrombin on synthetic substrates. J. Biol. Chem. 1954; 308: 85
   Google Scholar
• Sherry S., Troll W. The action of plasmin on synthetic substrates. J. Biol. Chem. 1954; 208: 95
   PubMed Web of Science ®Google Scholar
• Neurath H., Schwert G. W. The mode of action of the crystalline pancreatic proteolytic enzymes. Chem. Rev. 1950; 46: 69
   PubMed Web of Science ®Google Scholar
• Schwert G. W., Neurath H., Kaufman S., Snoke J. K. The specific esterase activity of trypsin. J. Biol. Chem. 1948; 172: 221
   PubMed Web of Science ®Google Scholar
• Colman R. W., Mason J. W., Sherry S. The kallikreinogen-kallikrein enzyme system of human plasma. Assay of components and observations in disease state. Ann. Intern. Med. 1969; 71: 763
   PubMed Web of Science ®Google Scholar
• Svendsen L., Blomback B., Blomback M., Olsson P. Synthetic chromogenic substrates for determination of trypsin, thrombin and thrombin-like enzymes. Thromb. Res. 1972; 1: 267
   Google Scholar
• Blomback M., Blomback B., Olsson P., Svendsen L. The assay of antithrombin using synthetic chromogenic substrate for thrombin. Thomb. Res. 1974; 5: 621
   PubMed Web of Science ®Google Scholar
• Chromogenic Peptide Substrates Chemistry and Clinical Applications, M. Scully, V. V. Kakkar. Churchill Livingstone, Edinburgh 1978
   Google Scholar
• Blomback B. Synthetic substrates and synthetic inhibitors. The use of chromogenic substrate in studies of the hemostatic mechanism. Haemostasis 1978; 7: 183
   PubMedGoogle Scholar
• Fareed J., Messmore H. L., Bermes E. W., Jr. New perspectives in coagulation testing. Clin. Chem. 1980; 26(10)1380
   PubMed Web of Science ®Google Scholar
• Svendsen L., Stocker K. Determination of protease activities with specifically constructed peptide-p-nitroanilide derivatives. New Methods for the Analysis of Coagulation Using Chromogenic Substrates, I. Witt. Walter de Gruyter, Berlin 1977; 23
   Google Scholar
• Mitchell G., Hudson P., Huseby R., Pochron S., Gargiulo R. J. Fluorescent substrate assay for antithrombin-III. Thromb. Res. 1978; 12: 219
   PubMed Web of Science ®Google Scholar
• Mitchell G., Hudson P., Huseby R. M. Assay for plasma heparin using a synthetic peptide substrate for thormbin. Thromb. Res. 1978; 13: 47
   PubMed Web of Science ®Google Scholar
• Claeson G., Aureil L., Karlsson G., Friberger P. Substrate structure and activity relationship. New Methods for the Analysis of Coagulation Using Chromogenic Substrates, I. Witt. Walter de Gruyter, Berlin 1977; 37
   Google Scholar
• Claeson G., Ekenstam B. O., Aureil L., Arwin H., Lundstrom I. New electric method to determine enzymatic activity. Determination of anti-thrombin in whole blood. Haemostasis 1978; 7: 135
   PubMedGoogle Scholar
• Bang N. U., Mattler L. E. Sensitivity and specificity of plasma serine protease chromogenic substrates. Haemostasis 1978; 7: 98
   PubMedGoogle Scholar
• Blomback B. Synthetic substrates and synthetic inhibitors. The use of chromogenic substrates in studies of the hemostatic mechanism. Haemostasis 1978; 7: 183
   PubMedGoogle Scholar
• Highsmith R. F., Rosenberg R. D. The inhibition of human plasmin by human antithrombin-heparin cofactor. J. Biol. Chem. 1974; 249: 4335
   PubMed Web of Science ®Google Scholar
• Telesford P., Semeraro N., Verstraete M., Collen D. The inhibition of plasmin by antithrombin-III-heparin complex in vitro in human plasma and during streptokinase therapy in man. Thromb. Res. 1975; 7: 669
   PubMed Web of Science ®Google Scholar
• Norman P. S., Hill B. M. Studies of the plasmin system. III. Physical properties of two plasmin inhibitors in plasma. J. Exp. Med. 1958; 108: 639
   PubMed Web of Science ®Google Scholar
• Ganrot P. O. The inhibition of plasmin activity by α2-macroglobulin. Clin. Chem. Acta 1967; 16: 328
   PubMed Web of Science ®Google Scholar
• Gans H., Tan B. H. α1-Antitrypsin, an inhibitor of thrombin and plasmin. Clin. Chem. Acta 1967; 17: 111
   PubMed Web of Science ®Google Scholar
• Harpel P. C., Cooper N. R. Studies on human plasma C1 inactivator enzyme interactions. I. Mechanisms of interaction with Cls, plasmin and trypsin. J. Clin. Invest. 1975; 55: 593
   PubMed Web of Science ®Google Scholar
• Harpel P. C. Plasmin inhibitor interactions: the effectiveness of α2-plasmin inhibitor in the presence of α2-macroglobulin. J. Exp. Med. 1977; 146: 1033
   PubMed Web of Science ®Google Scholar
• Crawford G. P. M., Ogston D., Douglas A. S. The contribution of plasma protease inhibitors to antiplasmin activity in man. Clin. Sci. Mol. Med. 1976; 51: 215
   PubMedGoogle Scholar
• Collen D. Identification and some properties of new fast-acting plasma inhibitor in human plasma. Eur. J. Biochem. 1976; 69: 209
   PubMedGoogle Scholar
• Fareed J., Messmore H. L., Orfei P., Gallagher J., Parvez Z., Bermes E. W. Comparative studies of the methodologies for the measurement of heparin cofactor (antithrombin-III). Clin. Chem. 1979; 25: 1076
   Web of Science ®Google Scholar
• Friberger P., Knos M., Gustavsson S., Auriel L., Claeson G. Methods for determination of plasmin, antiplasmin and plasminogen by means of substrate (S-2251). Haemostasis 1978; 7: 138
   PubMedGoogle Scholar
• Gallimore M. J., Amundsen E., Aasen A. O., Larsbraten M., Lyngass K., Svendsen L. Studies on plasma antiplasmin activity using a new plasmin specific chromogenic tripeptide substrate. Thromb. Res. 1979; 14: 51
   PubMed Web of Science ®Google Scholar
• Teger-Nielsson A. C., Friberger P., Gryzander E. Determination of a new rapid plasmin inhibitor in human blood by means of a plasmin specific tripeptide substrate. Scand. J. Clin. Lab. Invest. 1977; 37: 403
   PubMed Web of Science ®Google Scholar
• Lawson D. E., Mitchell G. A., Huseby R. M. A sensitive fluorescent assay for determining α2-plasmin inhibitor using a synthetic substrate. Thromb. Res. 1979; 14: 323
   PubMed Web of Science ®Google Scholar
• Tien A. N., Lie M., Abildgaard U. Assay of heparin in plasma using a chromogenic substrate. Thromb. Res. 1976; 8: 413
   PubMed Web of Science ®Google Scholar
• Larsen M. L., Abildgaard U., Teien A. N., Gjesdal K. Assay of plasma heparin using thrombin and the chromogenic substruate H-D-Phe-Pip-Arg-pNA (S-2238). Thromb. Res. 1978; 2: 285
   Google Scholar
• Bartl K. Effect of heparin-binding to thrombin on thrombin activity measured with a chromogenic substrate [letter]. Thromb. Res. 1978; 13(6)1141
   PubMed Web of Science ®Google Scholar
• Tien A. N., Lie M. Evaluation of an amidolytic heparin assay method: increased sensitivity by adding antithrombin-III. Thromb. Res. 1977; 10: 399
   PubMed Web of Science ®Google Scholar
• Van Wijk E. M., Kahle L. H., ten Cate J. W. A rapid manual chromogenic factor X assay. Thromb. Res. 1981; 22(5–6)681
   PubMed Web of Science ®Google Scholar
• Kirchoff B. R. J., Vermeer C., Hemker H. C. The determination of prothrombin using synthetic chromogenic substrates; choice of a suitable activator. Thromb. Res. 1978; 13: 219
   PubMed Web of Science ®Google Scholar
• Bergstrom K., Blomback M. Determination of plasma prothrombin with a reaction rate analyzer using a synthetic substrate. Thromb. Res. 1974; 4: 719
   PubMed Web of Science ®Google Scholar
• Tripodi A., Di Santo C., Mannucci P. M. A chromogenic assay of prothrombin compared with coagulation tests during anticoagulant therapy and disease. Ric. Clin. Lab. 1981; 11(3)215
   PubMedGoogle Scholar
• Stormorken H., Baklund A., Gallimore M., Ritland S. Chromogenic substrate assay of plasma kallikrein. With a note on its site of biosynthesis. Haemostasis 1978; 7: 75
   Google Scholar
• Bakland A., Gallimore H., Ritland S. Chromogenic substrate assay of plasma prekallikrein. Haemostasis 1978; 7: 69
   PubMedGoogle Scholar
• Aurell L., Friberger P., Karlsson G., Claeson G. A new sensitive and highly specific chromogenic peptide substrate for factor Xa. Thromb. Res. 1977; 11: 595
   PubMed Web of Science ®Google Scholar
• Witt I., Tritschler W., Bablok W. α2-Macroglobulin: values in serum and plasma with a chromogenic substrate. J. Clin. Chem. Clin. Biochem. 1981; 19(8)877
   Google Scholar
• Hayashi S., Yamada K. Assay of urokinase activity in plasma with a chromogenic substrate. Thromb. Res. 1981; 22(5–6)573
   PubMed Web of Science ®Google Scholar
• Svendsen L. Estimation of urokinase activity by means of a highly susceptible synthetic chromogenic peptide substrate. New Methods for the Analysis of Coagulation Using Chromogenic Substrates, I. Witt. Walter de Gruyter, Berlin 1977; 251
   Google Scholar
• Baughman D. J., Lytwyn A. Thrombin activation rate constant: one stage chromogenic assay for the extrinsic system. Thromb. Res. 1982; 26(1)
   PubMed Web of Science ®Google Scholar
• Fareed J., Messmore H. L., Walenga J. M., Kniffin J., Bermes E. W. Synthetic peptide substrates in the monitoring of anticoagulant and procoagulant therapy. J. Clin. Chem. Biochem. 1981; 19(8)663
   Google Scholar
• Vinazzer H. Diagnosis of intravascular coagulation by assays of activated factors X and XII with chromogenic substrates. Haematologica (Pavia) 1980; 65(5)636
   PubMed Web of Science ®Google Scholar
• Fareed J., Messmore H. L., Walenga J. M., Kniffin J., Bermes E. W. Status of amidolytic methods for the laboratory monitoring of antithrombotic and procoagulant therapy. Clin. Chem. 1981; 27(6)1107
   Web of Science ®Google Scholar
• Margaritella P., Deutsch E. Clinical use of a method for the determination of factor VII by a chromogenic substrate. Thromb. Res. 1981; 21(6)585
   PubMed Web of Science ®Google Scholar
• Ericksson E., Rosen S., Knos M., Friberger P. Chromogenic substrate method for the determination of factor VIII, endotoxin and plasminogen activator. Thromb. Haemos. 1981; 46(1)315
   Web of Science ®Google Scholar
• Seghatchian M. J. The usefullness of chromogenic substrates in the diagnosis of haemophilia and control of blood products. Chromogenic Peptide Substrates, M. F. Scully, V. V. Kakkar. Churchill Livingstone, London 1979; 102
   Google Scholar
• Byrne R., Link R. P., Castellino F. J. A kinetic evaluation of activated bovine blood coagulation factor IX toward synthetic substrates. J. Biol. Chem. 1980; 225(11)5336
   Google Scholar
• Vinazzer H. Assay of total factor XII and of activated factor XII in plasma with a chromogenic substrate. Thromb. Res. 1979; 14(1)155
   PubMed Web of Science ®Google Scholar
• Nieuwenhuizen W., Wijngaards G., Groeneveld E. Synthetic substrates and the discrimination between urokinase and tissue plasminogen activator activity. Thromb. Res. 1977; 11: 87
   PubMed Web of Science ®Google Scholar
• Huseby R. M., Clavin S. A., Smith R. E., Hull R. N., Smithwick E., Jr. Studies on tissue culture plasminogen activator II. The detection and assay of urokinase and plasminogen activator from LLLC-PK1 cultures (porcine) by the synthetic substrate Nα-Benzyloxycarbonyl-glycyl-glycyl-arginyl-4-methoxy-2-naphthylamide. Thromb. Res. 1977; 10: 679
   PubMed Web of Science ®Google Scholar
• Messmore H. L., Fareed J., Squillaci G., Walenga J. M., Bermes E. W. Application of synthetic substrates for the laboratory studies of ascitic fluids. Ann. Clin. Lab. Sci. 1980; 110(5)449
   Google Scholar
• Reich E. Serine enzymes released by cultured neoplastic cells. J. Exp. Med. 1978; 147: 745
   PubMed Web of Science ®Google Scholar
• Sandbery H., Andersen L. O. A highly sensitive assay of platelet factor 3 using a chromogenic substrate. Thromb. Res. 1979; 14: 113
   PubMed Web of Science ®Google Scholar
• Vinnazzer H. A simplified assay method for platelet factor 4 in plasma and in platelets with a chromogenic substrate. Haemos. 1978; 7: 352
   PubMedGoogle Scholar
• Thomas L. L., Sturk A., Kahle L. H., ten Cate J. W. Quantitative endotoxin determination in blood with a chromogenic substrate. Clin. Chem. Acta 1981; 116(1)63
   PubMed Web of Science ®Google Scholar
• Webster C. J. Principles of quantitative assay for bacterial endotoxins in blood that uses limulus lysate and a chromogenic substrate. J. Clin. Microbiol. 1980; 12: 644
   PubMed Web of Science ®Google Scholar
• Scully M. F., Newman Y. M., Clark S. E., Kakkar V. V. Evaluation of a chromogenic substrate method for endotoxin measurement. Thromb. Res. 1980; 20: 260
   Web of Science ®Google Scholar
• Ohno Y., Kato H., Iwanaga S., Takada K., Sakakibara S., Stenflo J. A new fluorogenic peptide substrate for vitamin K dependant blood coagulation factor bovine Protein C. J. Biochem. 1981; 90: 1387
   PubMed Web of Science ®Google Scholar
• Harpel P. C. A sensitive colorimetric method for the measurement of serum C1 inactivator using the substrate N-α-acetyl-L-lysine methyl ester. J. Immunol. 1970; 104: 1024
   PubMed Web of Science ®Google Scholar
• Schramm W., Penker W., Rupp A., Philapitsch A. Hypercoagulability-diagnostic value of C1-INA, in Abstr. F-167. Proc. 19th Congr. of Int. Soc. of Hematol., BudapestHungary, August, 1982, 381
   Google Scholar
• Bergstrom K., Blomback M. Determination of plasma prothrombin with a reaction rate analyzer using a synthetic substrate. Thromb. Res. 1974; 4: 719
   PubMed Web of Science ®Google Scholar
• Agent^tm, Quantichrom, Antithrombin-III Diagnostic kit product brochure. Abbott Laboratories Diagnostic Div., Abbott Park, Chicago, Ill
   Google Scholar
• Plasminogen Synthetic Substrate Assay for Determination of Plasmin and Plasminogen Activity in Plasma, Protopath^tm Product Brochure. Dade Division of American Hospital Supply Corporation, Miami, Fla
   Google Scholar
• Heparin Synthetic Substrate Assay for Determination of Heparin Activity in Plasma, Protopath^tm Product Brochure. Dade Division of American Hospital Supply Corporation, Miami, Fla
   Google Scholar
• AT-III Synthetic Substrate Assay for Determination of Antithrombin-III Activity in Plasma, Protopath^tm Product Brochure. Dade Division of American Hospital Supply Corporation, Miami, Fla
   Google Scholar
• Fareed J., Messmore H. L., Bermes E. W. New perspectives in coagulation testing. Clin. Chem. 1981; 26(10)1380
   Web of Science ®Google Scholar
• ødegard O. R. Evaluation of an amidolytic heparin cofactor assay method. Thromb. Res. 1975; 7: 351
   PubMed Web of Science ®Google Scholar
• Kahle L. H., Schipper H. G., Jenkins C. S. P., Tencate J. W. Antithrombin-III evaluation of an automated antithrombin-III method. Thromb. Res. 1978; 11: 1003
   Google Scholar
• Fagerhol M. K., Abildgaard U. Immunological studies on human antithrombin-III. Scand. J. Haematol. 1970; 7: 10
   PubMedGoogle Scholar
• Fareed J., Messmore H. L., Balis J. U. Current status of methodologies for antithrombin-III and heparin with the advent of peptide chromogenic substrates. Chromogenic Peptide Substrates, M. F. Scully, V. V. Kakkar. Churchill Livingstone, London 1979; 183
   Google Scholar
• Scully M. F., Kakkar V. V. Measurement of levels of degraded plasminogen during thrombolytic therapy. Chromogenic Peptide Substrates, M. F. Scully, V. V. Kakkar. Churchill Livingstone, London 1979; 141
   Google Scholar
• Progress in Chemical Fibrinolysis and Thrombolysis, J. F. Davidson. Raven Press, New York 1978–1983; 5 vol.
   Google Scholar
• Nilsson I. M., Hedner U., Pandolfi M. The measurement of fibrinolytic activities. Fibrinolytic and Antifibrinolyties, F. Markwardt. Springer-Verlag, Berlin 1978; 107
   Google Scholar
• Stormorken H. Relation of the fibrinolytic to the other biologic systems. Thromb. Haemost. 1975; 34: 378
   Google Scholar
• Collen D., Wiman B. Fast acting plasmin inhibitor in human plasma. Blood 1978; 51: 563
   PubMed Web of Science ®Google Scholar
• The Physiological Inhibitors of Blood Coagulation and Fibrinolysis, D. Collen, B. Wiman, M. Verstraete. Elsevier/North Holland, New York 1979
   Google Scholar
• Edy J., Decock F., Collen D. Inhibition of plasmin by normal and antiplasmin depleted human plasma. Thromb. Res. 1976; 8: 513
   PubMed Web of Science ®Google Scholar
• Parvez Z., Fareed J., Messmore H. L., Moncada R., Kniffin J., Bermes E. W., Jr. Measurement of fast-acting inhibitor (α2-antiplasmin) in plasma by immunologic and amidolytic methods. Clin. Chem. 1981; 27(6)1108
   Web of Science ®Google Scholar
• α₂-Antiplasmin Synthetic Substrate Assay for Plasma, Protopath^tm Product Brochure. Dade Division of American Hospital Supply Corporation, Miami, Fla 1981
   Google Scholar
• Erskine J. G., Walker I. D., Davidson J. F. Maintenance control of oral anticoagulant therapy by a chromogenic substrate assay for factor X. J. Clin. Pathol. 1980; 33: 445
   PubMed Web of Science ®Google Scholar
• Wijk E. M., van Kahle L. H., ten Cate J. W. Mechanized amidolytic technique for determination of factor X and factor X antigen and its application to patients being treated with oral anticoagulants. Clin. Chem. 1980; 26: 885
   PubMed Web of Science ®Google Scholar
• Lammle B., Bourameaus H., Marbet G. A., Eichlisberger R., Duckert F. Monitoring of oral anticoagulant by an amidolytic factor X assay. Thromb. Haemost. 1981; 44: 150
   Web of Science ®Google Scholar
• Jackson C. M., Suttie J. W. Recent developments in understanding the mechanism of vitamin K and vitamin K antagonist drug action and the consequences of vitamin K action in blood coagulation. Prog. Haematol. 1977; 10: 333
   PubMedGoogle Scholar
• Scully M. F., Kakkar V. V. Methods for semi-micro or automated determination of thrombin, antithrombin and heparin cofactor using the substrate H-d-Phe-Pip-Arg-P-Nitroanilide-2HC1. Clin. Chem. Acta 1977; 79: 595
   PubMed Web of Science ®Google Scholar
• Bergstrom K., Egberg N. Determination of vitamin K sensitive coagulation factors in plasma. Studies on three methods using chromogenic substrates. Thromb. Res. 1978; 12: 531
   PubMed Web of Science ®Google Scholar
• ødegard O. R., Rosenlund B., Ervick E. Automated antithrombin-III assay with a centrifugal analyzer. Haemost. 1978; 1: 202
   Google Scholar
• Kato M., Fujimaki M., Fukutake F., Maki A., Hibino M. Studies on nature of so-called antiplasmin measured by chromogenic substrate, S-2251 and its automatic determination with ABA-100. Thromb. Haemost. 1979; 42: 105
   Google Scholar
• Gray A. J., Uhlmeyer K. A., Fedor E. J. Quantichrom AT-III. Diagnostic kit for the quantification of total antithrombin-III in plasma. Thromb. Haemost. 1979; 42: 225
   Google Scholar
• Yamada K., Meguro T. Novel method of APTT using the chromogenic substrates for thrombin and an autoanalyzer. Thromb. Haemost. 1979; 42: 225
   Google Scholar
• Fareed J., Walenga J., Kelly J., Bermes E. W., Jr., Messmore H. L. Comparative evaluation of aca^tm methods for antithrombin-III, plasminogen and fibrinogen, Manuscript in preparation
   Google Scholar
• Walenga J., Kelly J., Fareed J., Messmore H. L., Bermes E. W., Jr. Performance characteristics of automated antithrombin-III, plasminogen and fibrinogen on the Du Pont's acatm system. Clin. Chem. 1982; 28(7)1585
   Web of Science ®Google Scholar
• Fareed J., Messmore H. L., Walenga J. M., Bermes E. W., Jr., Bick R. L. Laboratory evaluation of antithrombin-III: a critical overview of available methods for antithrombin-III measurements. Semin. Thromb. 1982; 8(104)288
   PubMedGoogle Scholar
• ødegard O. R., Teien A. N. Thromb. Res. 1976; 8: 173
   PubMed Web of Science ®Google Scholar
• Johnson A. J., Kline D. L., Alkjaersig N. Assay methods and standard preparation for plasmin, plasminogen, and urokinase in purified systems. Thromb. Haemost. 1969; 21: 259
   Google Scholar
• Collen D., de Cock F. Thrombin-antithrombin-III and plasmin-antiplasmin complexes as indicators of in vivo activation of the coagulation and/or fibrinolytic system. Thromb. Haemost. 1977; 38: 173
   Web of Science ®Google Scholar
• Yin E. T., Wessler S. Heparin accelerated inhibition of activated factor Xa by its plasma inhibitor. Biochem. Biophys. Acta 1970; 201: 387
   PubMedGoogle Scholar