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奇异柠檬酸杆菌ULA-27β-内酰胺酶。改进的纯化方法及一般特性。

Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties.

作者信息

Amicosante G, Oratore A, Franceschini N, Maccarrone M, Strom R, Galleni M, Frère J M

机构信息

Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Italy.

出版信息

Biochem J. 1988 Sep 15;254(3):885-90. doi: 10.1042/bj2540885.

Abstract

Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29,000). Their specificity spectrum was rather wide, since they hydrolysed some cephalosporins with kcat: values similar to those observed with the best penicillin substrates. Cloxacillin, methicillin and imipenem were hydrolysed very slowly. Hydrolysis of azthreonam could not be detected.

摘要

已从差异柠檬酸杆菌ULA - 27中纯化出两种染色体编码的β-内酰胺酶。它们表现出略有不同的等电点(6.8和6.2)以及非常相似的Mr值(约为29,000)。它们的底物特异性谱相当宽,因为它们水解一些头孢菌素的kcat值与用最佳青霉素底物观察到的值相似。氯唑西林、甲氧西林和亚胺培南水解非常缓慢。未检测到氨曲南的水解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba3e/1135165/6b412643a08b/biochemj00223-0249-a.jpg

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