METAL CHELATE AFFINITY-CHROMATOGRAPHY FOR THE PURIFICATION OF THE F420-REDUCING (NI,FE) HYDROGENASE OF METHANOSPIRILLUM-HUNGATEI

被引：4

作者：

CHOQUET, CG ^{[1
]}

SPROTT, GD ^{[1
]}

机构：

[1] NATL RES COUNCIL CANADA, INST BIOL SCI, OTTAWA K1A 0R6, ONTARIO, CANADA

来源：

JOURNAL OF MICROBIOLOGICAL METHODS | 1991年 / 13卷 / 02期

关键词：

HYDROGENASE; METAL CHELATE AFFINITY CHROMATOGRAPHY; METHANOSPIRILLUM-HUNGATEI; NI ENZYME;

D O I：

10.1016/0167-7012(91)90016-J

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Metal chelate affinity chromatography rapidly separated a soluble F420-reducing hydrogenase from its membrane-bound form, and from methyl-CoM reductase. The usefulness of the method depended on the metal chelated to the affinity matrix. Ni2+ and Zn2+ chelates were equally effective, a Cu2+ chelate inactivated the enzyme and Co2+ or Fe2+ chelates failed to bind the enzyme. A 3-day purification scheme was developed which resulted in > 40% recovery of the soluble F420-reducing hydrogenase activity, purified to > 90% electrophoretic homogeneity.

引用

页码：161 / 169

页数：9

共 20 条

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