PURIFICATION AND CHARACTERIZATION OF AN ACTOMYOSIN COMPLEX FROM ESCHERICHIA-COLI W3110

被引：2
|
作者：
FOSTER, SJ
机构：
来源：
FEMS MICROBIOLOGY LETTERS | 1993年 / 110卷 / 03期
关键词：
ACTOMYOSIN; CYTOSKELETAL ELEMENTS; ESCHERICHIA-COLI;
D O I：
10.1016/0378-1097(93)90118-L
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
An 'actomyosin' complex was purified from Escherichia coli W3110 using selective precipitation. The complex contains three major components of 19.5, 18.5 and 17 kDa. The 19.5- and 17-kDa proteins were purified by electroelution, peptide mapped and N-terminally sequenced. The structural gene for the 17-kDa protein was found to have been previously identified in an operon containing several other genes including the essential lpxA, lpxB and dnaE. The possible function of the 17-kDa protein and the other 'actomyosin' components is discussed.
引用
收藏
页码：295 / 298
页数：4
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