ABSENCE OF FERRIC ENTEROBACTIN RECEPTOR MODIFICATION ACTIVITY IN MUTANTS OF ESCHERICHIA-COLI K-12 LACKING PROTEIN-A

被引：34

作者：

FISS, EH

HOLLIFIELD, WC

NEILANDS, JB

机构：

[1] Department of Biochemistry, University of California, Berkeley

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 91卷 / 01期

关键词：

D O I：

10.1016/0006-291X(79)90578-3

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：

The modification activity for the ferric enterobactin receptor in the Triton X-100 solubilized outer membrane of Escherichia coli K-12 was adsorbed to a column of p-aminobenzamidine-//-sepharose and eluted with free benzamidine. Recombination of the dialyzed eluate with the filtrate from the column reinstituted conversion of the receptor from 81K to 81K*, the latter exhibiting an apparent molecular weight of 74,000 daltons in sodium dodecyl sulfate polyacrylamide gel analysis. The eluate from the p-aminobenzamidine column was shown to contain a component, coincident on gels with both protein and modification activity, which by mutational and other analyses appears to be identical with protein a of the outer membrane. © 1979.

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页码：29 / 34

页数：6

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