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[正常人纤维蛋白原苏黎世II的β和γ链分解为2种变体,每种变体的唾液酸含量不同]

[Resolution of Bbeta and gamma chains from normal human fibrinogen Zürich II into 2 variants with each differing sialic acid content].

作者信息

Gati W P, Straub P W

出版信息

Schweiz Med Wochenschr. 1976 Oct 2;106(40):1379.

PMID:1006261
Abstract

The gamma- and Bbeta-polypeptide chains of purified human fibrinogen (both pooled and single donor) have each been resolved into 2 major components: gammaL and gammaR, and BbetaL and BbetaR. They are similar in molecular weight (SDS-PAGE), but differ in sialic acid content, which approximates 2 and 1 residues per molecular of polypeptide in the L- and R-components respectively. Tryptic peptide maps of the L-and R- forms of the gamma chain showed differences within the small group of peptides containing the sialic acid residues. No differences between the peptide maps of BbetaL- and BbetaR-chains were found . A larger ratio of L:R in the gamma- and Bbeta-chains of dysfibrinogenemia fibrinogen "Zürich II" explains the higher content of sialic acid measured in the unmodified Zürich II fibrinogen molecule.

摘要

纯化的人纤维蛋白原(汇集的和单一供体的)的γ和β多肽链各自都已被解析为2个主要成分:γL和γR,以及βL和βR。它们的分子量相似(SDS-聚丙烯酰胺凝胶电泳),但唾液酸含量不同,L成分和R成分中每条多肽分子的唾液酸含量分别约为2个和1个残基。γ链L型和R型的胰蛋白酶肽图显示,在含有唾液酸残基的一小部分肽中存在差异。未发现βL链和βR链的肽图之间存在差异。异常纤维蛋白原血症纤维蛋白原“苏黎世II”的γ链和β链中L:R比例较高,这解释了在未修饰的苏黎世II纤维蛋白原分子中测得的较高唾液酸含量。

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