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β-半乳糖苷酶在可控孔径玻璃衍生物上的亲和层析

Affinity chromatography of beta-galactosidase on controlled-pore glass derivatives.

作者信息

Baum G

出版信息

J Chromatogr. 1975 Jan 29;104(1):105-11. doi: 10.1016/s0021-9673(01)85493-5.

DOI:10.1016/s0021-9673(01)85493-5
PMID:237008
Abstract

Several controlled-pore glass (CPG) derivatives were examined as supports for the affinity chromatographic purification of the enzyme beta-galactosidase. The competitive inhibitor p-aminophenyl-beta-D-thiogalactopyranoside was coupled to an azelaic acid and a malonic acid derivative of 750-A alkylamine CPG of 80-120 mesh and to an azelaic acid derivative of 550-A alkylamine CPG of 40-80 mesh. The latter derivative exhibited particularly good load capacity and separation efficiency; however, both arm lengths were effective. Hydrophobic interactions between the arm and the enzyme contribute to the separation.

摘要

研究了几种可控孔径玻璃(CPG)衍生物作为亲和色谱纯化β-半乳糖苷酶的载体。竞争性抑制剂对氨基苯基-β-D-硫代吡喃半乳糖苷与80-120目750-A烷基胺CPG的壬二酸和丙二酸衍生物以及40-80目550-A烷基胺CPG的壬二酸衍生物偶联。后一种衍生物表现出特别好的负载能力和分离效率;然而,两种臂长都是有效的。臂与酶之间的疏水相互作用有助于分离。

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