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Bulk isolation of the 20,000-Da light chain of smooth muscle myosin: separation of the unphosphorylated and phosphorylated species.

Authors
  • Sobieszek, A
Type
Published Article
Journal
Analytical biochemistry
Publication Date
Jul 01, 1988
Volume
172
Issue
1
Pages
43–50
Identifiers
PMID: 3189773
Source
Medline
License
Unknown

Abstract

The procedure of W. T. Perrie and S. V. Perry (1970, Biochem. J. 119, 31-38) has been improved and extended to allow a convenient large-scale isolation of the 20,000-Da light chain of vertebrate smooth muscle myosin. The method utilizes as source material tropomyosin-free actomyosin or myosin. The relatively pure light chain isolated from this material could be obtained in pure form by a single gel-filtration step. Separation of the unphosphorylated and phosphorylated light chain species was achieved by subsequent chromatography on a DEAE column. The solubility properties of this light chain, relevant to its use in myosin light chain kinase assays, were also established.

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