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由大肠杆菌中一种R因子介导的青霉素酶变体。

Variant of penicillinase mediated by an R factor in Escherichia coli.

作者信息

Sawai T, Takahashi K, Yamagishi S, Mitsuhashi S

出版信息

J Bacteriol. 1970 Nov;104(2):620-9. doi: 10.1128/jb.104.2.620-629.1970.

DOI:10.1128/jb.104.2.620-629.1970
PMID:4923065
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC285036/
Abstract

The penicillinase from an Escherichia coli strain harboring an R factor R(GN823) was purified and its properties were compared with those of a known type I penicillinase mediated by R factors. The molecular weight and S(20,w) of the enzyme were 22,600 and 2.42S, respectively. The isoelectric point of the enzyme was 6.9. These values are clearly different from those of type I penicillinase. The specific activity of the enzyme was 84,700 units per mg of the purified enzyme protein, which is about 20 times higher than that of the type I penicillinase. However, similarities were observed between the enzyme and the type I-penicillinase at optimal pH (6.5 to 7.0), optimal temperature (40 to 45C), substrate specificity, Michaelis constants for penicillins and cephaloridine, and effect of inhibitors. Furthermore, antiserum against type I penicillinase showed cross-reaction against this enzyme. The enzyme was named type Ib penicillinase, and the original type I penicillinase was renamed type Ia-penicillinase.

摘要

对携带R因子R(GN823)的大肠杆菌菌株产生的青霉素酶进行了纯化，并将其性质与已知的由R因子介导的I型青霉素酶的性质进行了比较。该酶的分子量和S(20,w)分别为22,600和2.42S。该酶的等电点为6.9。这些值与I型青霉素酶的值明显不同。该酶的比活性为每毫克纯化的酶蛋白84,700单位，约为I型青霉素酶的20倍。然而，在最佳pH（6.5至7.0）、最佳温度（40至45℃）、底物特异性、对青霉素和头孢菌素的米氏常数以及抑制剂的作用方面，观察到该酶与I型青霉素酶之间存在相似性。此外，抗I型青霉素酶的抗血清对该酶显示出交叉反应。该酶被命名为Ib型青霉素酶，原来的I型青霉素酶被重新命名为Ia型青霉素酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b128/285036/61ea99a83ebd/jbacter00583-0039-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b128/285036/61ea99a83ebd/jbacter00583-0039-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b128/285036/61ea99a83ebd/jbacter00583-0039-a.jpg

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本文引用的文献

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