Plasma factor XIII binds specifically to fibrinogen molecules containing gamma chains.
Plasma factor XIII binds specifically to fibrinogen molecules containing gamma chains.
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血浆因子 XIII 特异性结合含有 γ 链的纤维蛋白原分子。
DOI：
10.1021/bi9606206
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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;Meh,DA;Mosesson,MW
峰1和峰2纤维蛋白原的区别在于它们的γ链。峰1分子含有2个γ链，峰2分子含有1个γA链和1个γ‘链，后者含有一个20个氨基酸的延伸(γ’408−427)，取代了γ链的羧基末端4个氨基酸(γA408−411)。虽然血浆纤维蛋白原分子中存在γ‘链已知多年，但其功能仍不清楚。从血浆中提纯纤维蛋白原时，凝血因子XIII型酶原(A2B2)与之结合，经DEAE-纤维素离子交换层析从峰1中分离出来，仅在峰2中发现。当峰1纤维蛋白原+因子XIII或峰2纤维蛋白原+因子XIII的混合物用于DEAE柱时，峰1/因子XIII混合物在两个峰上洗脱，而峰2/因子XIII混合物在峰2处洗脱。对峰1/凝血因子XIII混合物的Superose 6进行凝胶筛选，得到两个蛋白质峰，第一个峰含有纤维蛋白原。大部分凝血因子XIII的活性在第二个峰洗脱，少量的活性出现在纤维蛋白原峰的后端。对峰2和凝血因子XIII的混合物进行凝胶筛选，得到一个单一的蛋白质峰，所有凝血因子XIII的活性都出现在纤维蛋白原峰的前沿。峰2纤维蛋白原与血浆凝血因子XIII之间的相互作用似乎是通过与凝血因子XIII的B亚基结合，因为胎盘或血小板因子XIII(A2)不含B亚基，在DEAE-纤维素层析上独立于峰2纤维蛋白原洗脱。结果表明，峰值2的纤维蛋白原γ‘链与血浆凝血因子XIII的B亚基具有显著的生理亲和力，通过这种相互作用，纤维蛋白原可作为循环血中血浆酶原的载体。
The difference between peak 1 and peak 2 fibrinogen lies in their γ chains. Peak 1 molecules contain 2 γAchains; peak 2 molecules contain 1 γAand 1 γ‘ chain, the latter of which contains a 20 amino acid extension (γ‘ 408−427) replacing the carboxyl-terminal 4 amino acids of the γAchain (γA408−411). While the existence of γ‘ chains in plasma fibrinogen molecules has been known for many years, their function remains unknown. When fibrinogen is purified from plasma, the factor XIII zymogen (A2B2) copurifies with it and is found only in the peak 2 fibrinogen when this fraction is separated from peak 1 fibrinogen by ion-exchange chromatography on DEAE-cellulose. Factor XIII alone applied to the same DEAE column elutes at a position between peak 1 and peak 2. When mixtures of peak 1 fibrinogen plus factor XIII or peak 2 fibrinogen plus factor XIII are applied to DEAE columns, the peak 1/factor XIII mixture elutes in two peaks, whereas the peak 2/factor XIII mixture elutes in the peak 2 fibrinogen position. Gel sieving on Superose 6 of peak 1/factor XIII mixtures results in two protein peaks, the first of which contains the fibrinogen. Most factor XIII activity elutes in the second peak with a small amount of activity emerging with the trailing end of the fibrinogen peak. Gel sieving of mixtures of peak 2 and factor XIII results in a single protein peak with all factor XIII activity emerging with the leading edge of the fibrinogen peak. The interaction between peak 2 fibrinogen and plasma factor XIII appears to be through binding to the B subunit of factor XIII since placental or platelet factor XIII (A2), which does not contain B subunits, elutes independently from peak 2 fibrinogen on DEAE-cellulose chromatography. The results indicate that peak 2 fibrinogen γ‘ chains have a physiologically significant affinity for the B subunits of plasma factor XIII and that through this interaction fibrinogen serves as a carrier for the plasma zymogen in circulating blood.