异青霉素N合成酶的纯化
Purification of isopenicillin N synthetase.
作者信息
Pang C P, Chakravarti B, Adlington R M, Ting H H, White R L, Jayatilake G S, Baldwin J E, Abraham E P
出版信息
Biochem J. 1984 Sep 15;222(3):789-95. doi: 10.1042/bj2220789.
Abstract
Isopenicillin N synthetase was extracted from Cephalosporium acremonium and purified about 200-fold. The product showed one major protein band, coinciding with synthetase activity, when subjected to electrophoresis in polyacrylamide gel. An isopenicillin N synthetase from Penicillium chrysogenum was purified about 70-fold by similar procedures. The two enzymes resemble each other closely in their Mr, in their mobility on electrophoresis in polyacrylamide gel and in their requirement for Fe2+ and ascorbate for maximum activity. Preliminary experiments have shown that a similar isopenicillin N synthetase can be extracted from Streptomyces clavuligerus.
摘要
异青霉素N合成酶从顶头孢霉中提取并纯化了约200倍。该产物在聚丙烯酰胺凝胶中进行电泳时，显示出一条与合成酶活性一致的主要蛋白带。通过类似的方法，产黄青霉中的异青霉素N合成酶被纯化了约70倍。这两种酶在分子量、在聚丙烯酰胺凝胶中的电泳迁移率以及对Fe2+和抗坏血酸的最大活性需求方面彼此非常相似。初步实验表明，一种类似的异青霉素N合成酶可以从克拉维链霉菌中提取。
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