PURIFICATION AND CHARACTERIZATION OF SALICYLATE HYDROXYLASE FROM PSEUDOMONAS-PUTIDA PPG7

被引：35
|
作者：
YOU, IS [1 ]
MURRAY, RI [1 ]
JOLLIC, D [1 ]
GUNSALUS, IC [1 ]
机构：
[1] UNIV ILLINOIS,DEPT BIOCHEM,URBANA,IL 61801
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 169卷 / 03期
关键词：
D O I：
10.1016/0006-291X(90)92000-P
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. © 1990.
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收藏
页码：1049 / 1054
页数：6
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