脆弱拟杆菌产生的新型β-内酰胺酶的特性
Properties of novel beta-lactamase produced by Bacteroides fragilis.
作者信息
Yotsuji A, Minami S, Inoue M, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1983 Dec;24(6):925-9. doi: 10.1128/AAC.24.6.925.
Abstract
Bacteroides fragilis strains were isolated from clinical specimens. B. fragilis G-237 was highly resistant to beta-lactam antibiotics due to beta-lactamase production. The purified enzyme from this strain gave a single protein band on polyacrylamide gel electrophoresis. The isoelectric point was 4.8, and the molecular weight was estimated to be 26,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme activity was inhibited by p-chloromercuribenzoate and iodine but not by clavulanic acid or sulbactam. The purified enzyme showed a unique substrate profile by hydrolyzing at a high rate most of the cephalosporins, including cephamycin derivatives, penicillins, and imipenem (formerly imipemide, N-formimidoyl thienamycin, or MK 0787).
摘要
脆弱翻译为
脆弱拟杆菌菌株从临床标本中分离得到。脆弱拟杆菌G-237因产生β-内酰胺酶而对β-内酰胺类抗生素高度耐药。从该菌株纯化得到的酶在聚丙烯酰胺凝胶电泳上呈现单一蛋白条带。其等电点为4.8，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计分子量为26000。该酶的活性受到对氯汞苯甲酸和碘的抑制，但不受克拉维酸或舒巴坦的抑制。纯化后的酶通过高速水解大多数头孢菌素（包括头霉素衍生物、青霉素和亚胺培南（原亚胺培南、N-甲酰亚胺基硫霉素或MK 0787））显示出独特的底物谱。
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