Title : Factor VIII and human platelet aggregation. III. Further studies on aggregation of humna platelets by neuraminidase-treated human factor VIII.

Pub. Date : 1976 Oct

PMID : 974043






4 Functional Relationships(s)
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Protein Name
Organism
1 When highly purified human factor VIII is submitted to agarose gel chromatography in the presence of 0.5 M CaCl2, the procoagulant activity (low molecular weight factor VIII, LMW-F VIII) is separated from the void volume protein (Vo-VIII). Sepharose cytochrome c oxidase subunit 8A Homo sapiens
2 When highly purified human factor VIII is submitted to agarose gel chromatography in the presence of 0.5 M CaCl2, the procoagulant activity (low molecular weight factor VIII, LMW-F VIII) is separated from the void volume protein (Vo-VIII). Sepharose cytochrome c oxidase subunit 8A Homo sapiens
3 When highly purified human factor VIII is submitted to agarose gel chromatography in the presence of 0.5 M CaCl2, the procoagulant activity (low molecular weight factor VIII, LMW-F VIII) is separated from the void volume protein (Vo-VIII). Sepharose cytochrome c oxidase subunit 8A Homo sapiens
4 When highly purified human factor VIII is submitted to agarose gel chromatography in the presence of 0.5 M CaCl2, the procoagulant activity (low molecular weight factor VIII, LMW-F VIII) is separated from the void volume protein (Vo-VIII). Sepharose cytochrome c oxidase subunit 8A Homo sapiens