Isolation of Fibrinogen Aα-Chain by Affinity Chromatography on Concanavalin A-Sepharose
Isolation of Fibrinogen Aα-Chain by Affinity Chromatography on Concanavalin A-Sepharose
复制标题
通过伴刀豆球蛋白 A-琼脂糖亲和层析分离纤维蛋白原 Aα-链
DOI：
10.1055/s-0038-1647050
复制
发表时间：
1988
影响因子：
6.7
通讯作者：
M. Furlan
中科院分区：
文献类型：
--
作者：
Christa Bögli;Anita Hofer;M. Furlan
Summary A method was developed for isolation of the Aa-chain from S-carboxamidomethylated fibrinogen. A mixture of the three constituent polypeptide chains of human fibrinogen was applied onto a column of concanavalin A-Sepharose. While the carbohydrate-free Aα-chain was not delayed on the affinity chromatography column, both glycosylated subunit chains, Bβ- and γ-chain, were adsorbed to the insolubilized lectin and were quantitatively eluted from the column with 0.2 M methyl-α-D-mannoside. SDS- electrophoresis on polyacrylamide gel was employed for analysis of chromatographic fractions. Complete recovery of the Aα-chain was observed. The described procedure is very simple and permits isolation of large amounts of pure Aα-chain from S-carboxamidomethylated fibrinogen.
