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由对羧苄青霉素高度耐药的铜绿假单胞菌菌株产生的β-内酰胺酶。

Beta-lactamases produced by a Pseudomonas aeruginosa strain highly resistant to carbenicillin.

作者信息

Labia R, Guionie M, Masson J M, Philippon A, Barthelemy M

出版信息

Antimicrob Agents Chemother. 1977 May;11(5):785-90. doi: 10.1128/AAC.11.5.785.

Abstract

A Pseudomonas aeruginosa strain isolated at Besançon Hospital, France, proved to be highly resistant to carbenicillin and showed a high hydrolytic activity toward this antibiotic. We clearly demonstrated that two beta-lactamases were synthetized: one of them, constitutive, has its enzymatic activity directed mainly toward penicillins, and carbenicillin appears to be its best substrate (higher V(max)); thus, this beta-lactamase is a "carbenicillinase" that differs from the well-known "TEM-like" enzymes. The isoelectric point of this carbenicillinase is 5.30 +/- 0.03. The other one is an inducible cephalosporinase, very similar to the cephalosporinases usually found in these organisms. Its isoelectric point is 8.66 +/- 0.04. These two enzymes have been separated by affinity chromatography and isoelectric focusing. The kinetic constants were measured by computerized microacidimetry.

摘要

从法国贝桑松医院分离出的一株铜绿假单胞菌,被证明对羧苄青霉素具有高度抗性,并且对这种抗生素表现出高水解活性。我们清楚地证明,该菌合成了两种β-内酰胺酶:其中一种是组成型的,其酶活性主要针对青霉素,羧苄青霉素似乎是其最佳底物(最大反应速度更高);因此,这种β-内酰胺酶是一种“羧苄青霉素酶”,与著名的“TEM样”酶不同。这种羧苄青霉素酶的等电点为5.30±0.03。另一种是诱导型头孢菌素酶,与通常在这些细菌中发现的头孢菌素酶非常相似。其等电点为8.66±0.04。这两种酶已通过亲和色谱法和等电聚焦法分离。动力学常数通过计算机化微量酸度测定法测量。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d59c/352075/d0aa81de9070/aac00299-0025-a.jpg

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