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PMID: 14332852 Published · ppublish English Journal Article

TEMPERATURE-SENSITIVE REPRESSION OF STAPHYLOCOCCAL PENICILLINASE.

Science (New York, N.Y.) ·Vol. 149 ·No. 3686 ·1965-08-20 ·Pages 877-9

COHEN S, SWEENEY H, LEITNER F

Abstract

In eight highly inducible strains of Staphylococcus aureus repression of the formation of penicillinase was temperature-sensitive under conditions suggesting direct thermal inactivation of the repressor. Restoration of repression required protein synthesis. These strains were resistant to benzylpenicillin and to many other antibiotics. One auxotrophic mutant had gredtly reduced temperature sensitivity but was still normally inducible. Six strains were relatively poorly inducible, exhibited a proportionately smaller increase in enzyme after exposure to elevated temperature, and were sensitive to antibiotics other than benzylpenicillin. Temperature sensitivity may be a useful character in studies of the physiology and genetics of the repression of staphylococcal penicillinase.

Keywords
ANTIBIOTICS BUFFERS CEPHALOSPORINS CULTURE MEDIA ENZYME REPRESSION EXPERIMENTAL LAB STUDY HEAT MUTATION PENICILLIN G PENICILLINASE PHARMACOLOGY PROTEIN METABOLISM PUROMYCIN STAPHYLOCOCCUS TEMPERATURE
MeSH Terms
Anti-Bacterial Agents Buffers Cephalosporins Culture Media Enzyme Repression Hot Temperature Mutation Penicillin G Penicillinase Pharmacology Proteins/metabolism Puromycin Research Staphylococcus Staphylococcus aureus Temperature
Chemicals
Anti-Bacterial Agents Buffers Cephalosporins Culture Media Proteins Puromycin Penicillinase Penicillin G
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
COHEN S
SWEENEY H
LEITNER F
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1965-08-20
Pages
877-9
Language
English
Region
United States
NLM ID
0404511
Subset
OM
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