PROTEIN CONFORMATIONAL ANNEALING - BINDING TO CYTOCHROME-C REFOLDS THE ACTIVE-SITE REGION OF RECOMBINANT CYTOCHROME-C PEROXIDASE

被引：5

作者：

HAKE, R ^{[1
]}

MCLENDON, G ^{[1
]}

CORIN, AF ^{[1
]}

机构：

[1] EASTMAN KODAK CO,RES LABS,ROCHESTER,NY 14650

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 172卷 / 03期

关键词：

D O I：

10.1016/0006-291X(90)91569-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

When initially isolated with heme reconstitution, recombinant cytochrome c peroxidase molecules exhibit a conformation, revealed by visible spectra which observably differ from the corresponding holo proteins isolated from yeast. Binding yeast iso-1 cytochrome c to these recombinant cytochrome c peroxidases (either in solution or via an affinity column) catalyses a local refolding of the recombinant proteins to a form that is indistinguishable from the native (yeast) protein. © 1990.

引用

页码：1157 / 1162

页数：6

共 13 条

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