嗜麦芽窄食单胞菌GN12873中一种诱导型头孢菌素酶的纯化及特性
Purification and properties of an inducible cephalosporinase from Pseudomonas maltophilia GN12873.
作者信息
Saino Y, Inoue M, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1984 Mar;25(3):362-5. doi: 10.1128/AAC.25.3.362.
Abstract
An inducible cephalosporinase was purified from Pseudomonas maltophilia GN12873. The pI was 8.4, and the molecular weight was ca. 56,000 by gel filtration or 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that this enzyme had two subunits. The optimal pH and optimal temperature were 7.5 and 45 degrees C, respectively. Enzyme activity was inhibited by clavulanic acid, sulbactam, cephamycin derivatives, carbapenem antibiotics, iodine, HgCl2, and p-chloromercuribenzoate. The enzyme showed a broad substrate profile, hydrolyzing cephaloridine, cefazolin, cefsulodin, penicillin G, ceftizoxime, and ampicillin at a high rate.
摘要
从嗜麦芽窄食单胞菌GN12873中纯化出一种诱导型头孢菌素酶。其等电点为8.4，通过凝胶过滤法测得分子量约为56,000，而通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法测得分子量为27,000，这表明该酶有两个亚基。最佳pH值和最佳温度分别为7.5和45℃。酶活性受到克拉维酸、舒巴坦、头孢霉素衍生物、碳青霉烯类抗生素、碘、HgCl2和对氯汞苯甲酸的抑制。该酶具有广泛的底物谱，能高效水解头孢菌素、头孢唑林、头孢磺啶、青霉素G、头孢唑肟和氨苄西林。
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