金黄色葡萄球菌PC1青霉素酶的活性位点。与底物喹那西林形成的特异性共价复合物的分离。
The active site of penicillinase from Staphylococcus aureus PC1. Isolation of a specific covalent complex with the substrate quinacillin.
作者信息
Virden R, Bristow A F, Pain R H
出版信息
Biochem J. 1975 Aug;149(2):397-401. doi: 10.1042/bj1490397.
Abstract
- The penicillinase-catalysed hydrolysis of quinacillin was quenched by addition of 5 m-guanidinium chloride or 1% (w/v) sodium dodecyl sulphate, and the quenched reaction mixture was dialysed exhaustively against solutions of the denaturant. 2. Irreversibly bound quinacillin was shown by titration with HgCl2 to be covalently attached to the protein by the beta-lactam carboxyl group. 3. The derivative was found to be stable over the pH range 3.5-8.5. 4. Chymotryptic hydrolysis of the product and subsequent fractionation showed that quinacillin was bound to one or possibly two peptides.
摘要
- 通过加入5M的氯化胍或1%（w/v）的十二烷基硫酸钠来终止青霉素酶催化的喹那西林水解反应，然后将终止后的反应混合物用变性剂溶液进行彻底透析。2. 用HgCl₂滴定表明，不可逆结合的喹那西林通过β-内酰胺羧基与蛋白质共价连接。3. 发现该衍生物在pH值3.5至8.5的范围内稳定。4. 对产物进行胰凝乳蛋白酶水解并随后进行分级分离，结果表明喹那西林与一种或可能两种肽结合。
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