铜绿假单胞菌中的质粒介导青霉素β-内酰胺酶
Plasmid-mediated penicillin beta-lactamases in Pseudomonas aeruginosa.
作者信息
Sawada Y, Yaginuma S, Tai M, Iyobe S, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1976 Jan;9(1):55-60. doi: 10.1128/AAC.9.1.55.
Abstract
A penicillin beta-lactamase (PCase) was extracted from Pseudomonas aeruginosa Rms139(+) and purified by means of column chromatography. The isoelectric point of Rms139 PCase was 5.7 and its molecular weight was 22,500 +/- 1,000. The optimal pH for the hydrolysis of benzylpenicillin was 7.0 to 7.5 and the optimal temperature was 45 C, with the PCase also showing high activity against carbenicillin. It is concluded that this enzyme is a new type of penicillin beta-lactamase different from the type I, II, or III R plasmid-mediated PCases reported previously.
摘要
从铜绿假单胞菌Rms139(+)中提取青霉素β-内酰胺酶（PCase），并通过柱色谱法进行纯化。Rms139 PCase的等电点为5.7，分子量为22,500±1,000。苄青霉素水解的最适pH为7.0至7.5，最适温度为45℃，该PCase对羧苄青霉素也表现出高活性。得出的结论是，这种酶是一种新型的青霉素β-内酰胺酶，不同于先前报道的I型、II型或III型R质粒介导的PCase。
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