Evidence of intramolecular cross-linked A alpha.gamma chain heterodimers in plasma fibrinogen.
Evidence of intramolecular cross-linked A alpha.gamma chain heterodimers in plasma fibrinogen.
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血浆纤维蛋白原中分子内交联的 A α.γ 链异二聚体的证据。
DOI：
10.1021/bi952264h
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Mosesson,MW
中科院分区：
文献类型：
--
作者：
Siebenlist,KR;Mosesson,MW
通过SDS−PAGE鉴定了一条迁移至二硫键还原人血浆纤维蛋白原γ二聚体位置附近的约105 kDa肽带，该人血浆纤维蛋白原由新鲜单个供体或过期血浆制备。该条带占Aα/γ链总数的0.2%，对凝血酶和纤溶酶敏感，与Aα或γ链的抗体反应，但不与Bβ链、纤溶酶原或因子XIII的抗体反应。氨基酸序列分析显示，该条带由共价交联的Aα·γ链异源二聚体组成，对应于Aα和γ链的双序列。通过二维SDS-PAGE和凝胶筛分色谱分离的单体组分的SDS-PAGE分析，Aα·γ异二聚体被鉴定为单体纤维蛋白原的组分，从而表明Aα·γ异二聚体通过分子内A α/γ链交联产生。
A peptide band of ∼105 kDa migrating near the γ dimer position of disulfide bond reduced human plasma fibrinogen prepared from fresh single donor or outdated plasma was identified by SDS−PAGE. The band, amounting to ∼2% of the total Aα/γ chain population, was thrombin and plasmin sensitive and reacted with antibodies to Aα or γ chains but not with antibodies to Bβ chains, plasminogen, or factor XIII. Amino acid sequencing revealed a double sequence corresponding to that of Aα and γ chains, indicating that the band consists of covalently cross-linked Aα·γ chain heterodimers. Aα·γ heterodimers were identified as a component of monomeric fibrinogen by two-dimensional SDS−PAGE and by SDS−PAGE analysis of the monomer fraction isolated by gel sieving chromatography, thus indicating that Aα·γ heterodimers arise byintramolecularAα/γ chain cross-linking.