Coagulation Proteins Showing Abnormal Electrophoretic Mobility in Commercial Concentrates of Factor VIII and Prothrombin Complex
作者:
V. Vicente,
I. Alberca,
I. Calles,
M. Manso,
A. Lopez Borrasca,
期刊:
Pathophysiology of Haemostasis and Thrombosis
(Karger Available online 1984)
卷期:
Volume 14,
issue 6
页码: 453-459
ISSN:1424-8832
年代: 1984
DOI:10.1159/000215105
出版商: S. Karger AG
关键词: Protein analysis, immunochemical;Factor VIII concentrates;Prothrombin complex concentrates;Coagulation proteins
数据来源: Karger
摘要:
Five commercial factor VIII (FVIII) concentrates and three prothrombin complex concentrates (PCC) were studied with reference to the qualitative evaluation of factors II, IX, fibronectin, α2-antiplasmin α2-AP), antithrombin III (AT-III) and subunits A and S of FXIII by crossed-immunoelectrophoresis (CIE) and von Willebrand factor antigen (vWF: Ag) by radio-CIE. This latter protein had a different pattern with the absence or a decrease of larger forms and the presence of a fast-moving precipitating peak, suggesting degradation of the vWF:Ag in FVIII concentrates. In contrast, the electrophoretic mobility of fibronectin, α2-AP and AT-III was normal. All PCC showed a more anodic mobility of factor IX. Α2-AP also exhibited a different electrophoretic pattern to that of normal plasma. Abnormality of AT-III was also found in heparin-binding studies. The techniques used in the purification procedures are probably the mechanism responsible for the partial denaturing of these prote
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