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从一株对青霉素敏感的金黄色葡萄球菌中分离β-内酰胺酶。

Isolation of beta-lactamase from a penicillin-susceptible strain of Staphylococcus aureus.

作者信息

Sachithanandam S, Lowery D L, Saz A K

出版信息

Antimicrob Agents Chemother. 1978 Feb;13(2):289-92. doi: 10.1128/AAC.13.2.289.

Abstract

It is generally accepted that strains of Staphylococcus aureus which are susceptible to penicillin G do not produce beta-lactamase. However, we have found that such a strain susceptible to 0.06 mug of penicillin per ml and 0.56 mug of methicillin per ml produces beta-lactamase(s) which hydrolyzes penicillin G, methicillin, 6-aminopenicillanic acid, and probably cephaloridine. The enzyme which is found only during very early log phase of the growth cycle is not inducible either by penicillin or methicillin and is cell bound and liberated only by disruption of the cell. The rate of enzymatic hydrolysis of methicillin was 60% that of benzylpenicillin. This finding suggests that the elaboration per se of beta-lactamase does not necessarily afford resistance to penicillin in this gram-positive-producing cell.

摘要

一般认为,对青霉素G敏感的金黄色葡萄球菌菌株不产生β-内酰胺酶。然而,我们发现,这样一株对每毫升0.06微克青霉素和每毫升0.56微克甲氧西林敏感的菌株产生了能水解青霉素G、甲氧西林、6-氨基青霉烷酸以及可能还有头孢菌素的β-内酰胺酶。仅在生长周期的非常早期对数期发现的这种酶既不能被青霉素也不能被甲氧西林诱导,它与细胞结合,只有通过细胞破裂才能释放出来。甲氧西林的酶促水解速率是苄青霉素的60%。这一发现表明,在这种革兰氏阳性菌产生细胞中,β-内酰胺酶的产生本身不一定赋予对青霉素的抗性。

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An introspective view of penicillinase.对青霉素酶的一种内省视角。
J Cell Physiol. 1970 Dec;76(3):397-403. doi: 10.1002/jcp.1040760318.

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