Subscribe to RSS
DOI: 10.1055/s-0038-1650090
Purification and Partial Characterization of a Hereditary Abnormal Antithrombin III Fraction of a Patient with Recurrent Thrombophlebitis
Publication History
Received 14 July 1980
Accepted 25 August 1980
Publication Date:
13 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198001/lookinside/thumbnails/10-1055-s-0038-1650090-1.jpg)
Summary
A relatively low heparin cofactor activity (0.60 U/ml) was observed in a patient with recurrent superficial thrombophlebitis of the left leg. However, the antigen concentration was in the normal range (1.04 U/ml) and the progressive antithrombin activity was normal. The crossed immunoelectrophoresis in presence of heparin in agarose gel separated the patient's AT-III antigen in 2 fractions with different mobilities. The patient's AT-III was purified for further characterization. The last step of the purification procedure, a heparin-agarose chromatography, led to a separation and a purification of 2 AT-III fractions with different heparin affinities: an abnormal AT-III with reduced heparin affinity and a normal AT-III with a heparin affinity similar to that of AT-III isolated from normal plasmas. Abnormal and normal AT-III share several identical properties as molecular weight, ability to form complexes with thrombin and progressive antithrombin activity.
-
References
- 1 Abildgard U. Highly purified antithrombin III with heparin cofactor activity prepared by disc electrophoresis. Scand J Clin Lab Invest 1968; 21: 89-91
- 2 Kurachi K, Fujikawa K, Schmer G, Davie EW. Inhibition of bovine factor IXa and factor Xa by antithrombin III. Biochem 1976; 15: 373-377
- 3 Yin ET, Wessler S, Stoll PJ. Identity of plasma activated factor X inhibitor with antithrombin III and heparin cofactor. J Biol Chem 1971; 246: 3712-3719
- 4 Rosenberg RD. The effect of heparin on factor XIa and plasmin. Thromb Diath Haemorrh 1974; 33: 51-62
- 5 Stead N, Kaplan AP, Rosenberg RD. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem 1976; 251: 6481-6488
- 6 Lahiri B, Bagdasarian A, Mitchell B, Talamo RC, Colman RW, Rosenberg RD. Antithrombin-heparin cofactor: an inhibitor of plasma kallikrein. Arch Biochem Biophys 1976; 175: 737-747
- 7 Miller-Andersson M, Borg H, Andersson LO. Purification of antithrombin III by affinity chromatography. Thromb Res 1974; 5: 439-452
- 8 Damus PS, Wallace GA. Purification of canine antithrombin III-heparin cofactor using affinity chromatography. Biochem Biophys Res Comm 1974; 61: 1147-1153
- 9 Thaler E, Schmer G. A simple two-step isolation procedure for human and bovine antithrombin II/III (heparin cofactor). A comparison of two methods. Brit. J Haematol 1975; 31: 233-243
- 10 Egeberg O. Inherited antithrombin deficiency causing thrombophilia. Thromb Diat Haemorrh 1965; 13: 516-530
- 11 Van der Meer J, Stoepman-van Dalen EA, Jansen JM S. Antithrombin III deficiency in a Dutch family. J Clin Path 1973; 26: 532-538
- 12 Shapiro SS, Prager D, Martinez J. Inherited antithrombin III deficiency associated with multiple thromboembolic phenomena. Blood 1973; 42: 1001 (Abstr.)
- 13 Marciniak E, Farley CH, Desimone PA. Familial thrombosis due to antithrombin III deficiency. Blood 1974; 43: 219-231
- 14 Sas G, Blasko G, Banhegyi D, Jako J, Palos LA. Abnormal antithrombin III (antithrombin III "Budapest") as a cause of a familial thrombophilia. Thromb Diath Haemorrh 1974; 32: 105-115
- 15 Stathakis NE, Papayannis AG, Antonopoulos M, Gardikas C. Familial thrombosis due to antithrombin III deficiency in a Greek family. Acta Haematol 1977; 57: 47-54
- 16 Mackie M, Bennett B, Ogston D, Douglas AS. Familial thrombosis: inherited deficiency of antithrombin III. Brit Med J 1978; 1: 136-138
- 17 Matsuo T, Ohki Y, Kondo S, Matsuo O. Familial antithrombin III deficiency in a Japanese family. Thromb Res 1979; 16: 815-831
- 18 Boyer C, Wolf M, Larrieu MJ. Formation of thrombin-antithrombin complexes in hereditary AT III deficiency. Study of 3 cases. Thromb Haemostas 1979; 42: 186 (Abstr.)
- 19 Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966; 15: 45-52
- 20 Ødegård OR. Evaluation of an amidolytic heparin cofactor method. Thromb Res 1975; 7: 351-360
- 21 Weber K, Osborn M. The reliability of molecular weight determinations by dodecylsulfate polyacrylamide gel electrophoresis. J Biol Chem 1969; 244: 4406-4412
- 22 Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads, J Biol Chem 1970; 245: 3059-3065
- 23 Owen WG, Esmon CT, Jackson CM. The conversion of prothrombin to thrombin. I. Characterization of the reaction products formed during the activation of bovine prothrombin. J Biol Chem 1974; 249: 594-605
- 24 Sas G, Pepper DS, Cash JD. Investigations on antithrombin III in normal plasma and serum. Brit J Haematol 1975; 30: 265-272
- 25 Sas G, Pepper DS, Cash JD. Further investigations on antithrombin in the plasma of patients with the abnormality of "antithrombin III Budapest". Thromb Diath Haemorrh 1975; 38: 494-503
- 26 Pepper DS, Banhegyi D, Cash JD. The different forms of antithrombin III in serum. Thromb Haemostas 1977; 38: 494-503
- 27 Penner JA, Hassouna H, Hunter MJ, Chockley MA. A clinically silent antithrombin III defect in an Ann Arbor family. Thromb Haemostas 1979; 42: 186 (Abstr.)
- 28 Tran TH, Bondeli C, Marbet GA, Duckert F. Reactivity of a hereditary abnormal antithrombin III fraction in the inhibition of thrombin and factor Xa. Thromb Haemostas 1980; 44: 92-95