КoMплeкcooбpaзoBaN;иe гeпapиN;a c фибpиN;ct;aбилизиpyющиM фaкt;opoM in vitro

Autor: Л.a. ЛяпиN, a.M. yльяN, Б.a. КyдpяMoB, A.M. Ulianov, B.A. Kudrjashov, L.A. Liapina
Rok vydání: 1973
Předmět:
Zdroj: Thrombosis Research. 3:589-603
ISSN: 0049-3848
DOI: 10.1016/0049-3848(73)90119-9
Popis: It has been found that heparin (Hp) forms a complex with fibrin stabilizing factor (FSF) in vitro. The formation of complex FSF-Hp has been testified by electrophoresis, analytical ultracentrifugation, spectral analysis in the regions of ultra-violet and ultra-red absorption and by study of differential spectrum of complex FSF-Hp. Maximum of specific biochemical activity of the complex FSF-Hp was estabilished when the weight relation between Hp and FSF reached 1:4, at pH 7,3. Complex FSF-Hp diminished specific activity when its formation was carried out in the conditions of raising or reducing weight ratio of Hp. The activity totally disappeared when ratio Hp:FSF was reached 1:1 or 1:15. Complex FSF-Hp obtained in optimal conditions acted as an inhibitor of polymerization (aggregation) of fibrin monomer. It also carried out the lysis of non-stabilized fibrin in the presence or absence of E-aminocaproic acid. The mentioned biochemical activity of complex FSF-Hp is very similar to one of complex fibrinogen-heparin, formation of which in vitro and in vivo and physiological significance we investigated before (2,3)
Databáze: OpenAIRE