Murata T, Minami S, Yasuda K, Iyobe S, Inoue M, Mitsuhashi S
J Antibiot (Tokyo). 1981 Sep;34(9):1164-70. doi: 10.7164/antibiotics.34.1164.
Cephalosporin beat-lactamase (cephalosporinase, CSase) was purified from a strain of Pseudomonas aeruginosa resistant to beta-lactam antibiotics. The purified enzyme preparation gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was about 34,000. The specific activity was 49.7 mumoles/minute/mg of protein of the purified enzyme for the hydrolysis of cephaloridine. The optimal pH and optimal temperature were about 8.0 and 40 degrees C, respectively. Its isoelectric point was 8.7. The enzyme activity was inhibited by iodine, some divalent ions, and some semisynthetic beta-lactam antibiotics, including cephamycin derivatives such as moxalactam and YM09330. Mouse antiserum obtained against the purified enzyme showed no cross-reaction with other types of beta-lactamase in neutralization test.
从一株对β-内酰胺类抗生素耐药的铜绿假单胞菌中纯化出头孢菌素β-内酰胺酶（头孢菌素酶，CSase）。纯化后的酶制剂在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上呈现单一蛋白条带，其分子量约为34,000。纯化酶水解头孢菌素的比活性为49.7微摩尔/分钟/毫克蛋白。最佳pH和最佳温度分别约为8.0和40℃。其等电点为8.7。该酶活性受到碘、一些二价离子以及一些半合成β-内酰胺抗生素（包括头霉素衍生物如莫西沙星和YM09330）的抑制。在中和试验中，针对纯化酶获得的小鼠抗血清与其他类型的β-内酰胺酶无交叉反应。
