从大肠杆菌W3310菌株中制备克级纯化的R因子介导的青霉素酶。
Preparation of gram quantities of a purified R-factor-mediated penicillinase from Escherichia coli strain W3310.
作者信息
Melling J, Scott G K
出版信息
Biochem J. 1972 Nov;130(1):55-62. doi: 10.1042/bj1300055.
Abstract
Purified penicillinase, in gram quantities, has been prepared from Escherichia coli strain W3310 by using methods developed to handle large amounts of material. The final product had a specific enzyme activity of 3.08 units/mug of protein, which was over twice as high as that reported previously (Datta & Richmond, 1966). The purified enzyme was similar to that from E. coli strain TEM, but different in molecular weight and some other respects. The differences observed may be a result of the greater purity obtained.
摘要
已采用为处理大量材料而开发的方法，从大肠杆菌W3310菌株中制备出了克级量的纯化青霉素酶。最终产物的比酶活性为每微克蛋白质3.08单位，这比之前报道的（达塔和里士满，1966年）高出两倍多。纯化后的酶与来自大肠杆菌TEM菌株的酶相似，但在分子量和其他一些方面有所不同。观察到的差异可能是由于获得了更高的纯度。
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