PMID: 2509202Oct 20, 1989Paper

Isolation and characterization of different activated forms of factor VIII, the human antihemophilic A factor

European Journal of Biochemistry
N BihoreauH Van de Pol

Abstract

Factor VIII was purified 1200-fold from commercial concentrates (Centre National de Transfusion Sanguine) by immunoaffinity chromatography using an anti-(80-kDa light chain) monoclonal antibody. The different molecular forms isolated were subsequently separated and analyzed using Fast Protein Liquid Chromatography and sodium dodecyl sulphate polyacrylamide gel electrophoresis analysis. The different factor-VIII forms obtained, consisted of 80-kDa light chains, each being associated with one more-or-less fragmented heavy chain ranging over 90-210 kDa. The specific activity of these different forms was 7000 U/mg. At different stages of activation of factor VIII by thrombin, various forms were separated and identified. Activated complexes were found to result from the association of the 70-kDa light chain (generated from the 80-kDa light chain) with heavy chains ranging over 90-210 kDa. Two different thrombin activation steps were characterized. The first step corresponding to the cleavage of the 80-kDa light chain led to a sixfold increase in the procoagulant activity, and yielded a stable activated intermediate form. Compared with normal factor VIII, the ratio of von Willebrand activity to factor-VIII activity, measured in the a...Continue Reading

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Citations

May 15, 1994·European Journal of Biochemistry·N BihoreauM P Fontaine-Aupart
Feb 14, 1991·European Journal of Biochemistry·S KrishnanC Roitsch
Feb 22, 2003·Blood·Chandrashekhara ManithodyAlireza R Rezaie
Apr 14, 1995·The Journal of Biological Chemistry·L M Regan, P J Fay

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