J. Lipid Res. Did you know there is a large type edition? Click here.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Witters, L. A.
Right arrow Articles by Vogt, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Witters, L. A.
Right arrow Articles by Vogt, B.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Lipid Research, Vol 22, 364-369, Copyright © 1981 by Lipid Research, Inc.

ARTICLES

A new method for the isolation of rat liver acetyl-CoA carboxylase

LA Witters and B Vogt

Rat liver acetyl-CoA carboxylase has been purified to homogeneity by a new method involving polyethylene glycol precipitation, and DEAE and Sepharose 4B chromatography. The final product displays a single band on SDS polyacrylamide gel electrophoresis of estimated molecular weight 240,000. This material contains 5.5 +/- 0.3 moles of alkali-labile phosphate per subunit and has a specific activity of 1.2 +/- 0.2 units per mg protein. As compared to previous purification procedures for the liver enzyme, this product has a higher phosphate content, lower specific activity, and an absence of major proteolysis. Trypsin digestion of 32P-labeled acetyl-CoA carboxylase from hepatocytes reveals that the 32P-labeled phosphorylation sites are extremely labile to proteolytic digestion. Potential modification of isolated liver acetyl-CoA carboxylase by proteolysis and/or dephosphorylation must be ascertained prior to in vitro enzymatic studies.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1981 by the American Society for Biochemistry and Molecular Biology.