Sawai T, Morioka K, Ogawa M, Yamagishi S
Antimicrob Agents Chemother. 1976 Aug;10(2):191-5. doi: 10.1128/AAC.10.2.191.
An inducible penicillinase was shown to be present in a strain of Aeromonas hydrophila subsp. hydrophila isolated from freshwater fish. Enzyme induction was observed with benzylpenicillin or 6-aminopenicillanic acid, and the enzyme was cell bound. The penicillinase was purified 50-fold from a crude cell extract. The molecular weight was estimated to be 23,000 by gel filtration. The pH and temperature optima for the enzyme activity were 8.0 and 35 degrees C, respectively. The penicillinase showed a unique substrate profile by hydrolyzing oxacillin about twice as rapidly as benzylpenicillin. The enzyme activity was weakly inhibited by sodium chloride but was not affected by p-chloromercuribenzoate. The property of penicillinase production by the A. hydrophila strain could not be transferred to Escherichia coli and also could not be eliminated from the bacteria by ethidium bromide treatment.
在从淡水鱼中分离出的嗜水气单胞菌嗜水亚种菌株中发现了一种可诱导的青霉素酶。用苄青霉素或6-氨基青霉烷酸可观察到酶的诱导作用，且该酶与细胞结合。青霉素酶从粗细胞提取物中纯化了50倍。通过凝胶过滤估计其分子量为23,000。该酶活性的最适pH和温度分别为8.0和35℃。该青霉素酶表现出独特的底物谱，水解苯唑西林的速度约为苄青霉素的两倍。酶活性受到氯化钠的微弱抑制，但不受对氯汞苯甲酸的影响。嗜水气单胞菌菌株产生青霉素酶的特性不能转移到大肠杆菌中，也不能通过溴化乙锭处理从细菌中消除。
