Document Type

Article

Publication Date

1-1-1977

Publication Title

Journal of Cell Biology

Abstract

Myosin and myosin light-chain kinase have been isolated and characterized from small quantities of normal and SV40-transformed, murine astrocytic neuroglial cells in culture and from intact normal mouse brain. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the astrocyte myosins revealed a heavy chain of 200,000 daltons and two light chains of 20,000 and 15,000 daltons. These myosins are similar to other cytoplasmic myosins. The astrocyte 20,000-dalton light chain can be phosphorylated by an endogenous myosin light- chain kinase which has properties similar to those of the myosin light-chain kinase found in human platelets. No differences were detected in either the astrocyte myosins or myosin light-chain kinases between (a) the normal and transformed cells, (b) the transformed cells grown at the permissive and nonpermissive temperatures, or (c) the SV40 wild-type and A-mutant transformants.

Keywords

myosin, phosphorylation, astrocytes, SV40 transformation

Volume

74

Issue

3

First Page

940

Last Page

949

DOI

10.1083/jcb.74.3.940

ISSN

00219525

Comments

Archived as published. Open access article.

Included in

Biology Commons

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.