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Thromb Haemost 1982; 47(02): 124-127
DOI: 10.1055/s-0038-1657145
DOI: 10.1055/s-0038-1657145
Original Article
Chromatography of Antihemophilic Factor on Diaminoalkane- and Aminoalkane-Derivatized Sepharose
Further Information
Publication History
Received 05 November 1981
Accepted 04 February 1982
Publication Date:
13 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198202/lookinside/thumbnails/10-1055-s-0038-1657145-1.jpg)
Summary
Antihemophilic factor was chromatographed on a homologous series of diaminoalkane- and aminoalkane-modified Sepharose beads. Both factor VIII procoagulant activity (VIII:C) and protein are retarded on these columns when compared to their elution on a column made of unmodified Sepharose. Longer chains bind VIII:C and protein more tightly than shorter chains. No bound activity could be eluted with ethylene glycol. Increasing ionic strength eluted VIII:C and protein from aminoalkane- as well as from alkane-Sepharose. It seems likely that hydrophobic, rather than ionic forces, are responsible for the binding of VIII:C to the latter carriers.
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References
- 1 Davie EW, Hanahan DJ. Blood coagulation proteins. In: The plasma proteins. Putnam FW. (ed.) 2. Vol. III 421-544 Academic Press; New York: 1977
- 2 Davie EW, Fujikawa K, Kurachi K, Kisiel K. The role of serine proteases in the blood coagulation cascade. Adv Enzymol 1979; 48: 277-318
- 3 Jackson CM, Nemerson Y. Blood coagulation. Annu Rev Biochem 1980; 49: 765-811
- 4 Weiss HJ, Kochwa S. Molecular forms of antihemophilic globulin in plasma, cryoprecipitate and after thrombin activation. Br J Haematol 1970; 18: 89-100
- 5 Weiss HJ, Phillips LL, Rosner W. Separation of sub-units of antihemophilic factor (AHF) by agarose gel chromatography. Throm-bos Diathes Haemorrh 1972; 27: 212-219
- 6 Owen WG, Wagner RH. Antihemophilic factor: separation of an active fragment following dissociation by salts or detergents. Throm-bos Diathes Haemorrh 1972; 27: 502-515
- 7 Rick ME, Hoyer LW. Immunologic studies of antihemophilic factor (AHF, factor VIII). V. Immunologic properties of AHF subunits produced by salt dissociation. Blood 1973; 42: 737-747
- 8 Weiss HJ, Hoyer LW. Von Willebrand factor: dissociation from antihemophilic factor procoagulant activity. Science 1973; 182: 1139-1151
- 9 Tran TH, Bounameaux H, Marbet GA, Duckert F. Dissociation du facteur VIII humain et recombinaison des fragments VIII-C et VIII-AG. Schweiz Med Wschr 1979; 109: 1029-1034
- 10 Austen DEG. The chromatographic separation of factor VIII on aminohexyl Sepharose. Br J Haematol 1979; 43: 669-674
- 11 Baugh R, Brown J, Sargeant R, Hougie C. Separation of human factor VIII activity from the von Willebrand’s antigen and ristocetin platelet aggregating activity. Biochim Biophys Acta 1974; 372: 360-367
- 12 Johnson AJ, MacDonald VE, Semar M, Fields JE, Schuck J, Lewis C, Brind J. Preparation of the major plasma fractions by solid-phase polyelectrolytes. J Lab Clin Med 1978; 92: 194-210
- 13 Perret BA, Furlan M, Kneubuehl F, Beck EA. Fractionation of individual, biologically active factor VIII multimers. Biochim Biophys Acta 1981; 669: 98-104
- 14 March SC, Parikh I, Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem 1974; 60: 149-152
- 15 Kolb WP, Kolb LM, Podack ER. C1q: Isolation from human serum in high yield by affinity chromatography and development of a highly sensitive hemolytic assay. J Immunol 1979; 122: 2103-2111
- 16 Chrétien R. Synthèses de diacides, d’aminoacides et d’une diamine à partir du furfural. Ann Chim (12e série) 1957; 2: 682-729
- 17 Vereinigte Glanzstoff-FabrikenA-G. Process for the production of aliphatic ω-chlorocarboxylic acid nitriles. Brit Pat. 1957 No. 768, 303
- 18 Lott WA, Krapcho J. Acid-addition quaternary salts and methods of preparing same. US Pat. 1957 No. 2, 813, 904
- 19 Moser S, Pflugshaupt R. Vergleichende Untersuchungen über die Bestimmung der Faktor-VIII-Aktivität. Schweiz Med Wschr 1974; 104: 1372-1373
- 20 Zuzel M, Nilsson IM, Åberg M. A method for measuring plasma ristocetin cofactor activity. Thromb Res 1978; 12: 745-754
- 21 Cooper HA, Reisner FF, Hall M, Wagner RH. Effects of thrombin treatment on preparations of factor VIII and the Ca++-dissodated small active fragment. J Clin Invest 1975; 56: 751-760
- 22 Brockway WJ, Fass DN. The nature of the interaction between ristocetin Willebrand factor and the factor VIII coagulant activity molecule. J Lab Clin Med 1977; 89: 1295-1305
- 23 Over J, Bouma BN, Sixma JJ, Bolhuis PA, Vlooswijk RAA. Heterogeneity of human factor VIII. III. Transitions between forms of factor VIII present in cryopredpitate and in cryosupematant plasma. J Lab Clin Med 1980; 95: 323-334
- 24 Broussard L, Harms WM, Shive W. Purification of the threonine-sensitive aspartokinase-homoserine dehydrogenase complex using chromatography on substituted Sepharose columns. Anal Biochem 1976; 72: 16-23
- 25 Visser J, Strating M. Separation of lipoamide dehydrogenase isoenzymes by affinity chromatography. Biochim Biophys Acta 1975; 384: 69-80
- 26 Shaltiel S. Hydrophobic chromatography. Methods Enzymol 1974; 34: 126-140