ESCHERICHIA-COLI ALKALINE-PHOSPHATASE FAILS TO ACQUIRE DISULFIDE BONDS WHEN RETAINED IN THE CYTOPLASM

被引：183

作者：

DERMAN, AI ^{[1
]}

BECKWITH, J ^{[1
]}

机构：

[1] HARVARD UNIV, SCH MED, DEPT MICROBIOL & MOLEC GENET, BOSTON, MA 02115 USA

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 23期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1128/jb.173.23.7719-7722.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The cysteines of the Escherichia coli periplasmic enzyme alkaline phosphatase, which are involved in disulfide bonds in the native enzyme, were found to be fully reduced when the protein was retained in the cytoplasm. Under these circumstances the cysteines remained reduced for at least several minutes after the synthesis of the protein was completed. This contrasted with the normally exported protein, wherein disulfide bonds formed rapidly. Disulfide bond formation accompanied export and processing. The implications of these findings for the inactivity of the enzyme in the cytoplasm are discussed.

引用

页码：7719 / 7722

页数：4

共 27 条

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