恶臭假单胞菌PpG7中水杨酸羟化酶的纯化与特性分析
Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7.
作者信息
You I S, Murray R I, Jollie D, Gunsalus I C
机构信息
Department of Biochemistry, University of Illinois, Urbana 61801.
出版信息
Biochem Biophys Res Commun. 1990 Jun 29;169(3):1049-54. doi: 10.1016/0006-291x(90)92000-p.
The salicylate hydroxylase from P. putida PpG7 was purified and characterized. The enzyme appears to be monomeric, and it showed one major band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent Mr of 45 kDa. The sequence of the first 25 amino acids of salicylate hydroxylase (PpG7) was determined. Also, the total amino acid composition of salicylate hydroxylase (PpG7) was obtained and compared with that of the known salicylate hydroxylase from P. putida.
对恶臭假单胞菌PpG7中的水杨酸羟化酶进行了纯化和表征。该酶似乎是单体，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上显示出一条主要条带，表观分子量为45 kDa。测定了水杨酸羟化酶（PpG7）前25个氨基酸的序列。此外，还获得了水杨酸羟化酶（PpG7）的总氨基酸组成，并与恶臭假单胞菌中已知的水杨酸羟化酶进行了比较。
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