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铜绿假单胞菌NCIB 9872环戊酮加氧酶的纯化及性质

Purification and properties of cyclopentanone oxygenase of Pseudomonas NCIB 9872.

作者信息

Griffin M, Trudgill P W

出版信息

Eur J Biochem. 1976 Mar 16;63(1):199-209. doi: 10.1111/j.1432-1033.1976.tb10222.x.

DOI:10.1111/j.1432-1033.1976.tb10222.x
PMID:4313
Abstract
  1. Cyclopentanone oxygenase from Pseudomonas NCIB 9872 has been purified some 40-fold. It gives a single peak in the ultracentrifuge and a single major protein band on polyacrylamide gels contaminated with about 5% of a slower migrating impurity. Flavin dissociates from the protein during electrophoresis. 2. The enzyme has a molecular weight of about 200000 and is a homopolymeric assemblage of either three of four subunits of molecular weight 54000-58000. 3. The prosthetic group is FAD and values of about 2.5 are typically obtained for the number of moles bound to each mole of holoenzyme. Some FAD probably dissociates during purification and it seems likely that each subunit binds one FAD in the undamaged protein.
摘要
  1. 来自假单胞菌NCIB 9872的环戊酮加氧酶已被纯化了约40倍。它在超速离心机中给出单一峰,在聚丙烯酰胺凝胶上给出单一主要蛋白带,但被约5%迁移较慢的杂质污染。黄素在电泳过程中从蛋白质上解离。2. 该酶的分子量约为200000,是由分子量为54000 - 58000的三个或四个亚基组成的同聚体组合。3. 辅基是FAD,每摩尔全酶结合的摩尔数通常约为2.5。在纯化过程中一些FAD可能解离,似乎每个亚基在未受损的蛋白质中结合一个FAD。

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