Related Experiment Videos
Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110
1Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
FEMS Microbiology Letters
|July 1, 1993
Abstract:
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.