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纤维蛋白原(Fbg)是一种血浆蛋白,在血液凝固中起着重要作用,现发现Fbg的Bβ链的364位和γ链52位天冬酰胺N端连有末端含唾液酸二天线寡糖,其糖链与Fbg凝固形成网状纤维蛋白有密切关系,后来进一步证实主要是Fbg末端结合的唾液酸(即Fbg结合唾液酸FSA)对纤维蛋白聚合铰链有影响.国外有关Fbg结合唾液酸在凝血中作用的研究已有不少报告,国内尚未见报道,本文通过对纯化的Fbg进行脱唾液酸前后的凝血酶时间测定比较,对Fbg结合唾液酸与Fbg凝血功能间的关系进行了实验研究.
Fibrinogen (Fbg) is a plasma protein that plays an important role in blood coagulation. It was found that the N-terminus at position 364 of the Bβ chain of Fbg and the asparagine at the 52-position of the γ chain were linked with the terminal sialylated two- , Its sugar chain and Fbg coagulation formation of reticular fibrin is closely related to later confirmed that the Fbg terminal binding of sialic acid (ie Fbg binding sialic acid FSA) on the fibrin polymerization hinge affect the foreign Fbg binding sialic acid in There are a lot of reports on the role of coagulation in China, but it has not been reported yet in our country. In this paper, the relationship between Fbg-binding sialic acid and Fbg coagulation function was studied through the comparison of the thrombin time of purified Fbg before and after asialo-sialic acid .