芳香黄杆菌产生的β-内酰胺酶的生化特性
Biochemical properties of beta-lactamase produced by Flavobacterium odoratum.
作者信息
Sato K, Fujii T, Okamoto R, Inoue M, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1985 Apr;27(4):612-4. doi: 10.1128/AAC.27.4.612.
Abstract
A constitutively produced beta-lactamase was purified from Flavobacterium odoratum GN14053. The purified enzyme gave a single protein band on polyacrylamide gel electrophoresis. The isoelectric point was 5.8, and the molecular weight was estimated to be about 26,000. The enzyme activity was inhibited by EDTA, iodine, p-chloromercuribenzoate, HgCl2, and CuSO4 but not by clavulanic acid, sulbactam, imipenem, and cephamycin derivatives. The enzyme showed a broad substrate profile, hydrolyzing oxyiminocephalosporins, cephamycins, imipenem, and some penicillins.
摘要
从芳香黄杆菌GN14053中纯化出一种组成型产生的β-内酰胺酶。纯化后的酶在聚丙烯酰胺凝胶电泳上呈现出单一蛋白条带。等电点为5.8，分子量估计约为26,000。该酶的活性受到EDTA、碘、对氯汞苯甲酸、氯化汞和硫酸铜的抑制，但不受克拉维酸、舒巴坦、亚胺培南和头孢霉素衍生物的抑制。该酶具有广泛的底物谱，能水解氧亚氨基头孢菌素、头孢霉素、亚胺培南和一些青霉素。
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