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耐甲氧西林金黄色葡萄球菌中青霉素结合蛋白2'的降解

Degradation of penicillin-binding protein 2' in methicillin-resistant Staphylococcus aureus.

作者信息

Sumita Y, Fukasawa M, Mitsuhashi S, Inoue M

机构信息

Episome Institute, Gunma, Japan.

出版信息

Chemotherapy. 1995 May-Jun;41(3):172-7. doi: 10.1159/000239340.

Abstract

We detected a novel protein with [14C]benzylpenicillin (PCG)-binding capacity and a molecular mass of about 60 kD in methicillin-resistant Staphylococcus aureus using a high concentration of [14C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin-binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of beta-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2'.

摘要

我们使用高浓度的[14C]苄青霉素(PCG)并延长反应时间,在耐甲氧西林金黄色葡萄球菌中检测到一种具有[14C]PCG结合能力且分子量约为60 kD的新型蛋白质。然而,荧光图谱显示青霉素结合蛋白2'(PBP2')的条带密度随孵育时间逐渐降低。60-kD蛋白质的出现与PBP2'条带密度的降低在化学计量上相关联,并且β-内酰胺对PBP2'和60-kD蛋白质的结合图谱相对应。这些结果表明60-kD蛋白质是PBP2'的降解产物。

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