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R因子介导的可水解苯唑西林的β-内酰胺酶:两个不同组别的证据。

R-factor-mediated beta-lactamases that hydrolyze oxacillin: evidence for two distinct groups.

作者信息

Dale J W, Smith J T

出版信息

J Bacteriol. 1974 Aug;119(2):351-6. doi: 10.1128/jb.119.2.351-356.1974.

Abstract

The enzymatic and molecular properties of 14 oxacillin-hydrolyzing beta-lactamases, all of them R-factor-specified, were studied, and two distinct groups were found. Four of the enzymes had a molecular weight of 24,000, were active against methicillin, and had an electrophoretic mobility of -0.1 cm/h. Eight enzymes had a molecular weight of 45,000, low activity against methicillin, and an electrophoretic mobility of +0.5 cm/h. The remaining two enzymes were similar to those of the second group in being relatively inactive against methicillin, but their molecular weight was lower (42,000) and their electrophoretic mobility was different (-0.1 cm/h). All the enzymes of both groups were sensitive to inhibition by sodium chloride. The two groups were not completely homogeneous in their enzymatic properties; seven possible subtypes could be recognized.

摘要

对14种均由R因子编码的水解苯唑西林的β-内酰胺酶的酶学和分子特性进行了研究,发现了两个不同的组。其中四种酶的分子量为24000,对甲氧西林有活性,电泳迁移率为-0.1 cm/h。八种酶的分子量为45000,对甲氧西林活性低,电泳迁移率为+0.5 cm/h。其余两种酶与第二组酶相似,对甲氧西林相对无活性,但分子量较低(42000),电泳迁移率不同(-0.1 cm/h)。两组所有的酶都对氯化钠抑制敏感。两组在酶学特性上并非完全同质;可识别出七种可能的亚型。

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