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PMID: 6969578 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and biochemical properties of beta-lactamase produced by Proteus rettgeri.

Antimicrobial agents and chemotherapy ·Vol. 18 ·No. 5 ·1980-11-00 ·Pages 687-90

Matsuura M, Nakazawa H, Inoue M, Mitsuhashi S

Abstract

beta-Lactamase produced by Proteus rettgeri was found to be a typical cephalosporin beta-lactamase on the basis of its substrate hydrolysis profile. The enzyme activity was enhanced by prior treatment with an inducer. The enzyme was purified 166-fold by carboxymethyl-Sephadex column chromatography which indicated that its molecular weight was 42,000 +/- 2,000 and its isoelectric point was 8.7. Cefoperazone, cefoxitin, cefusulodin, cefmetazole, cefotaxime, 6059-S, FK749, YM-09330, carbenicillin, and cloxacillin were stable to this enzyme and possessed the function of competitive inhibition, as shown by their affinity for the beta-lactamase. The enzyme activity was inhibited by iodine, p-chloromerburibenzoate, and HG2+ ion. Clavulanic acid and CP-45899 displayed poor inhibitory activity toward this enzyme. The optimal pH was 8.0, and the optimal temperature was 50 degrees C.

MeSH Terms
Anti-Bacterial Agents/pharmacology Bacterial Proteins/metabolism Drug Resistance, Microbial Molecular Weight Proteus/enzymology beta-Lactamases/isolation & purification,metabolism
Chemicals
Anti-Bacterial Agents Bacterial Proteins beta-Lactamases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Matsuura M
Nakazawa H
Inoue M
Mitsuhashi S
References (18)
18 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
DOI
10.1128/AAC.18.5.687
Published
1980-11-00
Pages
687-90
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC284076
Subset
IM
External Links
PubMed source DOI: 10.1128/AAC.18.5.687 PMC Full Text View journal details
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