A RIBOSOMAL PEPTIDASE FROM ESCHERICHIA COLI B

Author:

Matheson A. T.,Tsai C. S.

Abstract

Properties of a peptidase present in E. coli ribosomes have been studied. The enzyme is tightly bound to the ribosomes, as indicated by repeated washings and centrifugations, sucrose density gradient centrifugations, and electrophoresis on cellulose acetate. The level of enzyme activity in the 30 S particles is twice that found in the 50 S particles. When the ribosome structure is disrupted by enzymic or chemical means, the peptidase behaves similarly to the bulk of the ribosomal protein.

Publisher

Canadian Science Publishing

Subject

General Medicine

Cited by 39 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Leucine aminopeptidase in intracytoplasmic membranes ofAcinetobacter calcoaceticus;Journal of Basic Microbiology;1987

2. Purification and characterization of an intracellular N-terminal exopeptidase from Streptococcus durans;Biochimica et Biophysica Acta (BBA) - General Subjects;1984-07

3. Aminopeptidase I activities in several microorganisms;Canadian Journal of Biochemistry;1978-01-01

4. Cellular Location and Characteristics of Peptidase Enzymes in Lactic Streptococci;Journal of Dairy Science;1977-05

5. Peptides and Micro-Organisms;Advances in Microbial Physiology Volume 13;1976

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