Open AccessPurification and characterization of an ‘actomyosin’ complex from Escherichia coli W3110
Author(s) -
Foster Simon J.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06338.x
Subject(s) - chemistry , characterization (materials science) , biophysics , biology , nanotechnology , materials science
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.