巴曲酶
纤维蛋白
纤维蛋白原
凝血酶
化学
聚合
分子生物学
凝结
凝血酶时间
生物化学
生物物理学
免疫学
生物
医学
内科学
血小板
聚合物
部分凝血活酶时间
有机化学
作者
Keisuke Soya,Yuka Takezawa,Fumiko Terasawa,Nobuo Okumura
出处
期刊:PubMed
日期:2012-06-01
卷期号:60 (6): 499-505
摘要
We found and identified four heterozygous dysfibrinogenemias with AalphaR16H(CGT-->CAT) mutation in two families by coagulation tests and direct sequence analysis for PCR-amplified DNA fragments. Two dysfibrinogens were designated as fibrinogen Toyama and Adachi, according to the place of residence of proposituses, respectively. Patients' fibrinogen purified from plasma using immunoaffinity-chromatography was subjected to thrombin- or batroxobin-catalyzed fibrin polymerization, fibrinopeptide A (FPA) release, and clottability test. AalphaR16H-fibrinogen showed impaired thrombin or batroxobin-catalyzed fibrin polymerization in comparison with normal control fibrinogen. It is interesting that the period of protofibril formation of Toyama propositus was longest in those of four affected people. The clottability of AalphaR16H-fibrinogen was 66-70% with thrombin and higher than with batroxobin, 35-50%. In the same condition with fibrin polymerization, thrombin and batroxobin did not cleave the Aalpha16H-17G peptide-bonding, resulting in no release of variant FPA. From these results, we speculated that elongation of the two-stranded protofibril formation would be terminated by participation of the heterodimer fibrinogen molecules composed with a normal and an aberrant Aalpha-chain, and it would result in a decrease in fibrin polymerization. We speculated that the difference in the extent of impairment of fibrin polymerization among the patients might be caused by the different amount of heterodimers. Moreover, we also speculated that batroxobin-induced clottability was lower than thrombin-induced clottability, because batroxobin cannot induce the so-called "B-knob-b-hole" interaction, which enhances fibrin formation.
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