支气管败血波氏杆菌R因子介导的青霉素β-内酰胺酶的生化特性
Biochemical properties of a penicillin beta-lactamase mediated by R factor from Bordetella bronchiseptica.
作者信息
Yaginuma S, Terakado N, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1975 Sep;8(3):238-42. doi: 10.1128/AAC.8.3.238.
Abstract
The beta-lactamase specified by an R(te16) plasmid in Bordetella bronchiseptica was purified 200-fold by carboxymethyl-Sephadex column chromatography and electrofocusing. The enzyme has a molecular weight of 46,000 +/- 3,000 and an isoelectric point of 8.3 and was highly active against phenethicillin, oxacillin, and propicillin. The enzyme activity was inhibited by sodium chloride but not by ferrous ion. The maximal enzyme activity to benzylpenicillin was observed at pH 7.0 to 7.5 and at 40 C. It is concluded that this enzyme is different from the R-mediated beta-lactamases, i.e., the type I and type II beta-lactamases which have been classified in previous papers.
摘要
支气管败血波氏杆菌中由R(te16)质粒所编码的β-内酰胺酶，通过羧甲基-葡聚糖凝胶柱层析和电聚焦进行了200倍的纯化。该酶分子量为46,000±3,000，等电点为8.3，对苯氧乙基青霉素、苯唑西林和丙匹西林具有高活性。酶活性受氯化钠抑制，但不受亚铁离子抑制。在pH 7.0至7.5以及40℃时观察到对苄青霉素的最大酶活性。得出的结论是，该酶不同于R介导的β-内酰胺酶，即先前论文中分类的I型和II型β-内酰胺酶。
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