Affordable Access

Purification and characterization of an ‘actomyosin’ complex fromEscherichia coliW3110

Authors
Journal
FEMS Microbiology Letters
0378-1097
Publisher
Oxford University Press
Publication Date
Keywords
  • Actomyosin
  • Cytoskeletal Elements
  • Escherichia Coli
Disciplines
  • Biology

Abstract

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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Purification and characterization of an 'actomyosi...

on FEMS Microbiology Letters Jul 01, 1993

Mutational specificity of glyoxal, a product of DN...

on Mutation Research/Fundamental... Jan 01, 1997

Effect ofEscherichia coliW3110 on ruminal methanog...

on Animal Feed Science and Techno... Jan 01, 2005

Expression, Purification, and Characterization of...

on Protein Expression and Purific... Jan 01, 1997
More articles like this..