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一种由大肠杆菌中的R因子介导合成的青霉素酶的纯化及其性质

The purification and properties of a penicillinase whose synthesis is mediated by an R-factor in Escherichia coli.

作者信息

Datta N, Richmond M H

出版信息

Biochem J. 1966 Jan;98(1):204-9. doi: 10.1042/bj0980204.

Abstract
  1. The penicillinase (beta-lactamase) from Escherichia coli strain TEM has been purified and its activity against a range of penicillin and cephalosporin derivatives measured. 2. The enzyme shows little resemblance to penicillinases from Bacillus cereus, Bacillus licheniformis and Staphylococcus aureus. 3. The molecular weight of the enzyme is 16700+/-5%, which is about half the value obtained for other penicillinases. 4. The enzyme is most similar in properties to a crude preparation of a penicillinase from Klebsiella (Aerobacter) aerogenes, but clearly different from crude enzyme preparations from other strains of E. coli. 5. Since penicillinase synthesis in E. coli strain TEM is mediated by an R-factor known to infect many other species of Enterobacteriaceae, the appearance of similar enzymes in other Gramnegative species is not surprising.
摘要
  1. 已对来自大肠杆菌TEM菌株的青霉素酶(β-内酰胺酶)进行了纯化,并测定了其对一系列青霉素和头孢菌素衍生物的活性。2. 该酶与蜡状芽孢杆菌、地衣芽孢杆菌和金黄色葡萄球菌的青霉素酶几乎没有相似之处。3. 该酶的分子量为16700±5%,约为其他青霉素酶所得值的一半。4. 该酶在性质上与产气克雷伯菌(产气气杆菌)青霉素酶的粗制品最为相似,但与其他大肠杆菌菌株的粗酶制品明显不同。5. 由于大肠杆菌TEM菌株中青霉素酶的合成是由一种已知可感染许多其他肠杆菌科物种的R因子介导的,因此在其他革兰氏阴性物种中出现类似的酶并不奇怪。

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