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标题：Factor VIII Recombination After Dissociation by CaCl2
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作者：Herbert A. Cooper ; Thomas R. Griggs ; Robert H. Wagner 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：8
页码：2326-2329
DOI：10.1073/pnas.70.8.2326
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Factor VIII is a large protein molecule of molecular weight 2,000,000 or larger that elutes in the void volume on agarose gel chromatography. It has been shown previously that high concentrations of alkali halides and, more specifically, 0.25 M Ca2+ dissociate the molecule into a large carrier protein and a small fragment that retains the factor VIII activity. Factor VIII was prepared from normal canine plasma collected in sodium oxalate and heparin and adsorbed with BaSO4. Results with Ca2+ dissociation were the same as those obtained with fraction prepared from canine plasma collected in sodium citrate. The addition of 0.1 M {varepsilon}-aminocaproic acid in the dissociation step had no effect. Fractionation of canine hemophilic plasma produced preparations without activity, and no activity was found when these inert preparations were dissociated with Ca2+. These results indicate that the Ca2+ dissociation is a true dissociation and not caused by enzymatic degradation by plasmin, thrombin, or activated factors VII, IX, or X. The apparent molecular weight of the small active fragment of factor VIII determined by gel chromatography was about 100,000. Finally, when the large carrier protein and the small active fragment of factor VIII were separated by gel chromatography, mixed, and dialyzed free of Ca2+, they recombined to form a large active molecule that appeared in the void volume on agarose gel chromatography.
关键词：canine plasma fractions ; antihemophilic factor ; gel chromatography ; molecular weight