30
Views
21
CrossRef citations to date
0
Altmetric
Original Article

In Vitro Evaluation of Heparin Fractions: Old vs. New Methods

, , &
Pages 361-389 | Published online: 02 Jul 2009

References

  • Baugh R. F., Hougie C. Biochemistry of blood coagulation. Recent Advances in Blood Coagulation, L. Poller. Churchill Livingstone, London 1977; 1
  • Bjork I., Lindahl U. Mechanism of the anticoagulant action of heparin. Mol. Cell Biochem. 1982; 48: 161
  • Pitney W. R. Heparin therapy and its laboratory control. Br. J. Haematol. 1970; 18: 499
  • Teien A. N., Lie M. Heparin assay in plasma: a comparison of five clotting methods. Thromb. Res. 1975; 7: 777
  • Deykin D. Monitoring heparin therapy. JAMA 1982; 247: 3136
  • Simon T. L., Smith K. L. Heparin assays. Methods Hemalol. 1983; 119
  • Gutman S. I., Didisheim P., Markowitz H. Two new artifacts in automated coagulation testing. Am. J. Clin. Pathol. 1980; 73: 583
  • Brandt J. T., Triplett D. A. Laboratory monitoring of heparin. Effect of reagents and instruments on the activated partial thromboplastin time. Am. J. Clin. Pathol. 1981; 76: 530
  • Basu G., Gallus A., Hirsh J., Cade J. A prospective study of the value of monitoring heparin treatment with the activated partial thromboplastin time. New Engl. J. Med. 1972; 287: 324
  • Bick R. L., McClain B. J. A comparison of five activated partial thromboplastin times and the activated clotting time during heparin therapy. Thromb. Hemost. 1983; 50: 236, (Abstr. 736)
  • Banez E. I., Triplett D. A., Koepke J. Laboratory monitoring of heparin therapy. The effect of different salts of heparin on the activated partial thromboplastin time. Am. J. Clin. Pathol. 1980; 74(Suppl.)530
  • Poller L., Thomson J. M., Palmer M. K. Measuring partial thromboplastin time, an assessment of the performance in serial studies. J. Clin. Pathol. 1976; 35: 251
  • U.S. Pharmacopeia XX. U.S. Pharmacopeial Convention, Inc., Rockville, Md, 20th revision
  • Teien A. N., Abildgäard U. On the value of the activated partial thromboplastin time (APTT) in monitoring heparin therapy. Thromb. Hemost. 1976; 35: 592
  • Silverglade A. Biological equivalence of beef lung and hog mucosal heparins. Curr. Ther. Res. 1975; 18: 91
  • Brozovic M., Bangham D. R. Standards for heparin. Heparin: Strucure, Function, and Clinical Implications, R. Bradshaw, S. Wessler. Plenum Press, New York 1975; 163
  • Baltes B. J., Diamond S., D'Agostino R. Comparison of anticoagulant activity of two preparations of purified heparin. Clin. Pharmacol. Ther. 1973; 14: 287
  • Gomez-Perez F. Anticoagulant activity of two commercially available heparin preparations. J. Clin Pharmacol. 1972; 12: 413
  • Barrowcliffe T. W., Johnson E. A., Eggleton C. A., Thomas D. P. Anticoagulant activities of lung and mucous heparins. Thromb. Res. 1977; 12: 27
  • Ofosu F. A., Cerskus A. L., Hirsh J., Smith L. M., Modi G. J., Blajchman M. A. The inhibition of the anticoagulant activity of heparin by platelets, brain phospholipids, and tissue factor. Br. J. Haematol. 1984; 57: 229
  • Jaques L. B., Wollin A. A modified method for the colorimetric determination of heparin. Can. J. Physiol. Pharmacol. 1967; 45: 787
  • Edstrom R. D. A colorimetric method for the determination of mucopolysaccharides and other acidic polymers. Anal. Biochem. 1969; 29: 421
  • Lam L. H., Silbert J. E., Rosenberg R. D. The separation of active and inactive forms of heparin. Biochem. Biophys. Res. Commun. 1976; 69: 570
  • Bitter T., Muir H. M. A modified uronic acid carbazole reaction. Anal. Biochem. 1962; 4: 330
  • Galambox J. T. The reaction of carbazole with carbohydrates. Anal. Biochem. 1967; 19: 119
  • Balazs E. A., Bernsten O., Karossa J. An automated method for the determination of hexosamines. Anal. Biochem. 1965; 12: 559
  • Feingold D., Roden L., Forsee T. Heparin biosynthesis. Chemistry and Biology of Heparin, R. L. Lundblad, W. V. Brown, K. G. Mann, H. R. Roberts. Elsevier/North-Holland, New York 1981; 157
  • Sache E., Maillard M., Bertrand H. Studies on a highly potent anticoagulant high molecular weight fraction isolated from porcine heparin. Chemistry and Biology of Heparin, R. L. Lundblad, W. V. Brown, K. G. Mann, H. R. Roberts. Elsevier/North-Holland, New York 1981; 645
  • Godal H. D. The assay of heparin in thrombin systems. Scand. J. Clin. Lab. Invest. 1961; 13: 153
  • Barrowcliffe T. W., Johnson E. A., Eggleton C. A., Kemball-Cook G., Thomas D. P. Anticoagulant activities of high and low molecular weight fractions. Br. J. Haematol 1979; 41: 573
  • Lane D. A., MacGregor I. R., van Ross M., Cella G., Kakkar V. V. Molecular weight dependence of the anticoagulant properties of heparin. Intravenous and subcutaneous administration of fractionated heparins in man. Thromb. Res. 1979; 16: 651
  • Holmer E., Mattsson C., Nilsson S. Anticoagulant and antithrombotic effects of heparin and low-molecular-weight heparin fragments in rabbits. Thromb. Res. 1982; 25: 475
  • Carter C. J., Kelton J. G., Hirsh J., Gent M. Relationship between the antithrombotic and anticoagulant effects of low molecular weight heparin. Thromb. Res. 1981; 21: 169
  • McGowan F. X., Nash P. V., Bjornsson T. D. Assay-dependent kinetics of heparin: evidence for rapid in vivo activation of heparin. Br. J. Clin. Pharmacol. 1983; 16: 677
  • Holmer E., Kurachi K., Soderstrom G. The molecular weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa and kallikrein by antith-rombin. Biochem. J. 1981; 193: 395
  • Friberger P., Egberg N., Holmer E., Hellgren M., Blömback M. Antithrombin assay—the use of human or bovine thrombin and the observation of a second heparin cofactor. Thromb. Res. 1982; 25: 433
  • Cade J. F., Buchanan M. R., Boneu B., Ockelford P., Carter C. J., Cerskus A. L., Hirsh J. A comparison of the antithrombotic and haemorrhagic effects of low molecular weight heparin fractions: the influence of the method of preparation. Thromb. Res. 1984; 35: 613
  • Eggleton C. A., Barrowcliffe T. W., Merton R. E., Thomas D. P. In vitro and in vivo studies of the anti-Xa activity of heparin. Thromb. Res. 1981; 24: 319
  • Yin E. T., Salsgiver W. J., Tangen O. Normal human plasma contains a naturally occurring antagonist of activated factor X inhibitor (antithrombin III) activity. Thromb. Res. 1979; 15: 557
  • Ofosu F. A., Modi G. J., Smith L. M., Cerskus A. L., Hirsh J., Blajchman A. Heparin sulfate and dermatan sulfate inhibit the generation of thrombin activity in plasma by complementary pathways. Blood 1984; 64: 727
  • Ofosu F. A., Modi G., Cerskus A. L., Hirsh J., Blajchman M. A. Heparin with low affinity to antithrombin III inhibits the activation of prothrombin in normal plasma. Thromb. Res. 1982; 28: 487
  • Abildgäard U., Larsen M. L. Assay of dermatan sulfate cofactor (heparin cofactor II) activity in human plasma. Thromb. Res. 1984; 35: 257
  • Hojima Y., Cochrane C. G., Wiggins R. C., Austen K. F., Stevens R. L. In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood 1984; 63: 1453
  • Tollefsen D. M., Majerus D. W., Blank M. K. Heparin cofactor II: purification and properties of a heparin-dependent inhibitor of thrombin in human plasma. J. Biol. Chem. 1982; 257: 2162
  • Ofosu F. A., Blajchman M. A., Modi G., Cerskus A. L., Hirsh J. Activation of factor X and prothrombin in antithrombin-III depleted plasma: the effects of heparin. Thromb. Res. 1981; 23: 331
  • Fischer A. M., Dautzenberg M. D., Aurousseau M. H., Beguin S., Goudermand J., Hemker H. C. Comparison between the effect of Pentosan polysulphate heparin and antithrombin III injections in antithrombin III deficient patients. Thromb. Res. 1985; 37: 295
  • Fischer A. M., Tapon-Bretaudiere J., Bros A., Josso F. Respective roles of antithrombin III and alpha 2 macroglobulin in thrombin inactivation. Thromb. Haemost. 1981; 45: 51
  • Variel E. G., Boyte-Boye H., Toulemonde F., Doutremepuich C., Marsh N. A., Gaffney P. J. Heparin and a low molecular weight fraction enhances thrombolysis and by its pathway exercises a protective effect against thrombosis. Thromb. Res. 1983; 30: 219
  • Bara L., Kher A., Samama M. Lower enhancement in vitro of AT III-mediated antiplasmin activity by low molecular weight heparin, PK 10169 (MW 5,000) than by unfractionated heparin. Hemo-stasis 1984; 14: 219
  • Hennink W. E., Klerx J. P. A. M., van Dijk H., Feijen J. Complement inhibitory and anticoagulant activities of fractionated heparins. Thromb. Res. 1984; 36: 281
  • Casu B., Johnson E. A., Mantovani M., Mulloy B., Oreste P., Peseador R., Prino G., Torro G., Zoppetti G. Correlation between structure, fat-clearing and anticoagulant properties of heparins and heparan sulphates. Drug Res. 1983; 33: 135
  • Kecskés E., Büki K. G., Bauer P. I., Machovich R., Horváth I. Interaction of heparin with lipoproteins—role of the complex in the inactivation of thrombin and plasmin. Thromb. Haemost. 1983; 49: 138
  • Eldor A., Weksler B. B. Heparin and dextran sulfate antagonize PGI2 inhibition of platelet aggregation. Thromb. Res. 1979; 16: 617
  • Niewiarowski S., Rucinski B., James P., Lindahl U. Platelet antiheparin proteins and antithrombin III interact with different binding sites on heparin molecule. FEBS Lett. 1979; 102: 75
  • Mastacchi R., Stanzani L., Barbanti M., Montecchi L., Bianchini P. Interaction of heparin and heparin fractions with human platelets. Thromb. Res. 1982; 28: 275
  • Laghi Pasini F., Pasqui A. L., Ceccatelli L., Capecchi P. L., Orrico A., Di Perri T. Heparin inhibition of polymorphonuclear leukocyte activation in vitro. A possible pharmacological approach to granulocyte-mediated vasular damage. Thromb. Res. 1984; 35: 527
  • Choay J., Lormeau J. C., Petitou M., Sinay P., Casu B., Oreste P., Torri G., Gatti G. Anti Xa active heparin oligosaccharide. Thromb. Res. 1980; 18: 573
  • Cifoneili J. A. The relationship of molecular weight, and sulfate content and distribution to anticoagulant activity of heparin preparations. Carbohydr. Res. 1974; 37: 145
  • Laurent T. C., Tengblad A., Thunberg L., Hook M., Lindahl U. The molecular weight dependence of the anticoagulant activity of heparin. Biochem. J. 1978; 175: 691
  • Andersson L. O., Barrowclirfe T. W., Holmer E., Johnson E. A., Söderström G. Molecular weight dependency of the heparin potentiated inhibition of thrombin and activated factor X. Effect of heparin neutralization in plasma. Thromb. Res. 1979; 15: 531
  • Graham D. T., Pomeroy A. R. Relative activities of heparin fractions obtained by gel chromatography. Thromb. Hemost. 1980; 42: 1598
  • Hurst R. E., Menter J. M., West S. S., Settine J. M., Coyne E. H. Structural basis for the anticoagulant activity of heparin 1. Relationship to the number of charged groups. Biochemistry 1979; 18: 4283
  • Hurst R. E., Poon M. C., Griffith M. J. Structure-activity relationships of heparin. Independence of heparin charge density and antithrombin-binding domains in thrombin inhibition by antithrombin and heparin cofactor II. J. Clin. Invest. 1983; 72: 1042
  • Rosenberg R. D., Armand G., Lam L. Structure function relationships of heparin species. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 3065
  • Choo I. H. F., Didisheim P., Doerge M. L., Johnson M. L., Bach M. L., Melchert L. M., Johnson W. J., Taylor W. F. Evaluation of a heparin assay method using a fluorogenic synthetic peptide substrate for thrombin. Thromb. Res. 1982; 25: 115
  • Denson K. W. E., Bonnar J. The measurement of heparin. A method based on the potentiation of anti-factor Xa. Thromb. Diath. Haemorrh. 1973; 30: 471
  • Friberger P. Properties of the “Coatest” heparin assay. Heparin. New Biochemical and Medical Aspects, I. Witt. Walter de Gruyter & Co., Berlin 1982; 117
  • Handeland G. F., Abildgäard U. Assay of unfractionated and LMW heparin with chromogenic substrates: twin methods with factor Xa and thrombin. Thromb. Res. 1984; 35: 627
  • Scully M., Kakkar V. V. Chromogenic Substrates. Churchill Livingstone, EdinburghScotland 1978
  • Fareed J., Walenga J. M., Messmore H. L., Bermes E. W., Jr. Synthetic substrates in hemostatic testing. CRC Crit. Rev. Lab. Sci. 1983; 19: 71
  • Messmore H. L., Fareed J., Kniffin J., Squillaci G., Walenga J. Synthetic substrate assays of the coagulation enzymes and their inhibitors. Comparison with clotting and immunological methods for clinical and experimental usage. Ann. N. Y. Acad. Sci. 1981; 370: 787
  • Odegard O. R., Abildgärd U., Lie M. Antifactor Xa measured with amidolytic methods. Haemostasis 1976; 5: 265
  • Van Wijk E. M., Kahle I. H., Wiebosch M., ten Cate J. W. Optimization of a mechanized amidolytic factor X assay; influence of reaction conditions and reagents. Clin. Chem. 1981; 27: 918
  • Michaud A., Aiach M. Application des substrats chromogenès à la surveillance biologique de l'héparinotheraphie. Pharmacol. Biol. 1982; 16: 29
  • Kapke G. F., Feld R. D., Witte D. L., Owen W. G. Esterolytic method for determination of heparin in plasma. Clin. Chem. 1981; 27: 526
  • Larsen M. L., Abildgäard U., Teien A. N., Gjesdal K. Assay of plasma heparin using thrombin and the chromogenic substrate H-D-Phe-Pip-Arg-pNA (S-2238). Thromb. Res. 1978; 13: 285
  • Mitchell G. A., Garginlo R. J., Huseby R. M., Lawson D. E., Pochron S. P., Sehuanes J. A. Assay for plasma heparin using a synthetic peptide substrate for thrombin. Introduction of the fluorophore, isophthalic acid, dimethyl ester. Thromb. Res. 1978; 13: 47
  • Teien A. N., Lie M., Abildgäard U. Assay of heparin in plasma using chromogenic substrate for activated factor X. Thromb. Res. 1976; 8: 413
  • Bartl K., Dorsch E., Lill H., Ziegenhorn J. Determination of the biological activity of heparin by use of a chromogenic substrate. Thromb. Haemost. 1979; 42: 1446
  • Aiach M., Michaud A., Capron L., Fiessinger J. N. Determination of factor X and heparin with chromogenic substrate. Acta Chir. Scand. 1982; 509(Suppl.)109
  • Brown J. E., Baugh R. F., Hougie C. The inhibition of the intrinsic generation of activated factor X by heparin and hirudin. Thromb. Res. 1980; 17: 267
  • Ofosu F., Blajchman M. A., Hirsh J. The inhibition by heparin of the intrinsic pathway activation of factor X in the absence of antithrombin-III. Thromb. Res. 1980; 20: 391
  • Kakkar V. V. Prevention of postoperative venous thromboembolism by a new low molecular weight heparin fraction. Nouv. Rev. Fr. Hematol. 1984; 26: 277
  • Kakkar V. V., Djazaeri B., Fok J., Fletcher M., Scully M. F., Westwick J. Low-molecularweight heparin and prevention of postoperative deep vein thrombosis. Br. Med. J. 1982; 284: 375
  • Schmitz-Heuber U., Asbeck F., van de Loo J. In vivo studies on the inhibition of coagulation by fractionated heparin and by a heparin analogue. II. Effects of a heparin analogue. Thromb. Haemosti. 1981; 46: 617
  • Walenga J. M., Bara L., Samama M. M., Fareed J. Amidolytic antifactor Xa assays in the laboratory evaluation of heparin and low molecular weight fractions. Semin. Thromb. Hemost. 1985; 11(2)104
  • Walenga J. M., Fareed J., Messmore H. L. Newer avenues in the monitoring of antithrombotic therapy: the role of automation. Semin. Thromb. Hemost. 1983; 9: 346
  • Yin E. T., Wessler S., Butler J. V. Plasma heparin: a unique, practical submicrogram-sensitive assay. J. Lab. Clin. Med. 1973; 81: 298
  • Sturzebecher J., Markwardt F., Wagner G., Boigt B. Are synthetic inhibitors able to improve factor Xa assays using peptide substrates?. Thromb. Res. 1982; 26: 221
  • Hoppensteadt D., Fareed J., Walenga J. M., Emanuele R. M. Validity of serine protease inhibition tests in the in vitro and in vivo assessment of the action of heparin and its fractions. Fed. Proc. Fed. Am. Soc. Exp. Biol. 1984; 43: 606
  • Ockelford P. A., Carter C. J., Mitchell L., Hirsh J. Discordance between the anti-Xa activity and the antithrombotic activity of an ultra low molecular weight fraction. Thromb. Res. 1982; 28: 401
  • Van Mourik J. A. The significance of fibrinopeptide A (FPA) in the diagnosis of low-grade intravascular coagulation and venous thromboembolism. Haematologia (Pavia) 1981; 66: 259
  • Mombelli G., Roux A., Haeberli A., Straub P. W. Comparison of 125I fibrinogen kinetics and fibrinopeptide A in patients with disseminated neoplasias. Blood 1982; 60: 381
  • Peuscher F. W., van Aken W. G., Flier O. T., Stoerman-van Dalen E. A., Cremer-Goote T. M., van Mourik J. A. Effect of anticoagulant treatment measured by fibrinopeptide A (FPA) in patients with venous thromboembolism. Thromb. Res. 1980; 18: 33
  • Yudelman I., Greenberg J. Factors affecting fibrinopcptide-A levels in patients with venous thromboembolism during anticoagulant therapy. Blood 1982; 49: 787
  • Emanuele R. M., Fareed J., Hoppensteadt D., Walenga J. M. Development of fibrinopeptide A generation tests in the evaluation and the monitoring of the action of heparin and its low molecular weight fractions. Semin. Thromb. Hemost. 1984; 10: 243
  • Johnson P. C., Ware J. A., Cliveden P. B., Smith M., Dvorah A. M., Salzman E. W. Measurement of ionized calcium in blood platelets with the photo protein aequorin: comparison with Quin Z, in press
  • Yin E. T., personal communication
  • Obzanky D. M., Pierson-Perry J. F., Mizzer J. P. Development and analytic performance of an automated assay for effective plasma heparin activity. Clin. Chem. 1985; 31(6)977

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.