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核酸与蛋白质的疏水亲和层析。II. 三苯甲基琼脂糖固定化酶的活性

Hydrophobic affinity chromatography of nucleic acids and proteins. II. Activity of trityl Sepharose immobilized enzymes.

作者信息

Cashion P, Javed A, Sathe G, Ali G

出版信息

Nucleic Acids Symp Ser. 1980(7):173-89.

PMID:6166924
Abstract

A variety of nucleic acid synthetic and degradative enzymes and proteases are shown to bind to trityl sepharose columns and, for the most part, retain moderate amounts of activity for periods of days to weeks. Non-covalent hydrophobic interactions are believed to be largely responsible for the observed binding and maintenance of activity. In addition the hydrophobic binding mechanism of poly A to trityl sepharose columns under a variety of conditions is compared with that to nitrocellulose columns and contrasted with that of dT cellulose columns.

摘要

已表明多种核酸合成酶、降解酶和蛋白酶可与三苯甲基琼脂糖柱结合,并且在很大程度上能在数天至数周的时间内保持一定量的活性。非共价疏水相互作用被认为是观察到的结合及活性维持的主要原因。此外,还比较了在各种条件下多聚腺苷酸与三苯甲基琼脂糖柱的疏水结合机制,以及与硝酸纤维素柱的结合机制,并与脱氧胸苷纤维素柱的结合机制进行了对比。

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