Purification of three gamma-chains with different molecular weights from normal human plasma fibrinogen.
Purification of three gamma-chains with different molecular weights from normal human plasma fibrinogen.
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从正常人血浆纤维蛋白原中纯化三种不同分子量的伽马链。
DOI：
10.1016/0304-4165(84)90253-8
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Marder,VJ
中科院分区：
文献类型：
--
作者：
Francis,CW;Keele,EM;Marder,VJ
纯化了三种分子量不同的正常人血浆纤维蛋白原γ链。血浆纤维蛋白原通过离子交换色谱在DEAE-Sephacel上分离成三个分子群体，每个群体具有独特的γ-链组成。经还原和S-羧甲基化后，通过DEAE-Sephacel离子交换层析分离每个色谱峰中的纤维蛋白原多肽链，并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行鉴定。Aα、Bβ和最小的γ-链（γ50）在逐渐升高的离子强度下洗脱，但Aα、Bβ和γ 50链的洗脱位置对于来自三种不同色谱级分的纤维蛋白原是相同的。第二个色谱峰中唯一的纤维蛋白原γ链（γ55）在高于γ 50链的离子强度下洗脱，而仅包含在纤维蛋白原第三个色谱峰中的最大γ链（γ57.5）在最高离子强度下洗脱。在第二个和第三个峰中溶解纤维蛋白原所需的较高离子强度被溶解它们特有的γ-链所需的较高离子强度所抵消，表明三种纤维蛋白原组分的γ-链组成解释了它们与离子交换树脂的差异结合。用神经氨酸酶去唾液酸后，三种γ-链形式之间的电泳迁移率差异得以保持，表明SDS-聚丙烯酰胺凝胶电泳上的差异迁移不是由于唾液酸含量的变化。
Three forms of the normal human plasma fibrinogen γ-chain which differ in molecular weight have been purified. Plasma fibrinogen was separated by ion exchange chromatography on DEAE-Sephacel into three populations of molecules, each with a unique γ-chain composition. Following reduction andS-carboxymethylation, the fibrinogen polypeptide chains in each chromatographic peak were separated by ion exchange chromatography on DEAE-Sephacel and identified following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The Aα, Bβ and smallest γ-chain (γ50) eluted at progressively higher ionic strengths, but the elution positions of Aα, Bβ andγ50chains were identifcal for fibrinogen from each of the three different chromatographic fractions. The unique γ chain of fibrinogen in the second chromatographic peak (γ55) eluted at an ionic strength higher than that of theγ50chain, while the largest γ-chain (γ57.5), which was contained only in the third chromatographic peak of fibrinogen, eluted at the highest ionic strength. The higher ionic strengths needed to elute fibrinogen in the second and third peaks was paralleled by the higher ionic strengths needed to elute the γ-chains unique to them, suggesting that the γ-chain composition of the three fibrinogen fractions accounted for their differential binding to the ion exchange resin. Following desialation with neuraminidase, the differences in electrophoretic mobilities between the three γ-chain forms was maintained, indicating that differential migration on SDS-polyacrylamide gel electrophoresis was not due to variation in sialic acid content.
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人纤维蛋白原γ链变体（γ）的羧基末端氨基酸序列。
影响因子：
2.9
作者：
C. Wolfenstein‐Todel;M. Mosesson
通讯作者：
M. Mosesson
人纤维蛋白原异质性：A α 起源链的分布和电荷特征。
DOI：
--
发表时间：
1978
期刊：
Journal of Laboratory and Clinical Medicine
影响因子：
--
作者：
D. Galanakis;M. Mosesson;N. Stathakis
通讯作者：
N. Stathakis
人纤维蛋白原S-羧甲基衍生物链的制备与分离
影响因子：
3.5
作者：
G. Murano;B. Wiman;M. Blombäck;B. Blombäck
通讯作者：
B. Blombäck
纤维蛋白聚合位点的定位
影响因子：
6.7
作者：
S. Olexa;A. Budzynski
通讯作者：
A. Budzynski
使用基于胺掺入的新测定法对纤维蛋白稳定因子进行诊断和遗传学研究。
影响因子：
15.9
作者：
L. Lorand;T. Urayama;J. W. De Kiewiet;H. Nossel
通讯作者：
H. Nossel