The Journal of antibiotics · 1981
Purification and properties of cephalosporinase from Pseudomonas aeruginosa.
СтатьяНазвание и аннотация: Перевод пока не подготовлен
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Murata T, Minami S, Yasuda K, Iyobe S, Inoue M, Mitsuhashi S
Аннотация
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.