戈尔曼军团菌产生的β-内酰胺酶的生化特性。
Biochemical properties of beta-lactamase produced by Legionella gormanii.
作者信息
Fujii T, Sato K, Miyata K, Inoue M, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1986 May;29(5):925-6. doi: 10.1128/AAC.29.5.925.
Abstract
beta-Lactamase was purified from a strain of Legionella gormanii. The molecular weight of the purified enzyme was 25,000, and its isoelectric point was 10.5. The enzyme hydrolyzed oxyiminocephalosporins, cephamycins, penicillins, and imipenem. The enzyme activity was inhibited by EDTA, Hg2+, and Cu2+, but not by clavulanic acid, sulbactam, or imipenem.
摘要
β-内酰胺酶是从戈氏军团菌菌株中纯化得到的。纯化酶的分子量为25,000，其等电点为10.5。该酶可水解氧亚氨基头孢菌素、头霉素、青霉素和亚胺培南。酶活性受到EDTA、Hg2+和Cu2+的抑制，但不受克拉维酸、舒巴坦或亚胺培南的抑制。
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