J. Lipid Res.
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Killenberg, P. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Killenberg, P. G.
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 19, 24-31, Copyright © 1978 by Lipid Research, Inc.

ARTICLES

Measurement and subcellular distribution of choloyl-CoA synthetase and bile acid-CoA:amino acid N-acyltransferase activities in rat liver

PG Killenberg

An improved method for assaying choloyl-CoA synthetase activity (E.C. 6.2.1.7) and two methods for specific measurement of bile acid- CoA:amino acid N-acyltransferase activity (E.C. 2.3.1) are described. The methods are shown to be reproducible, linear with respect to time and enzyme protein, and result in estimates of enzymic activity that conform to the theoretical stoichiometry of the individual reactions. Utilizing these methods, the subcellular distribution of the rat liver enzymic activity catalyzing the formation of glycine and taurine conjugates of bile acids is shown. Choloyl-CoA synthetase is associated with the microsomal membranes and bile acid-CoA:amino acid N- acyltransferase activity with the postmicrosomal supernatant. No significant amino acid N-acyltransferase activity is present in the lysosome fraction. These studies provide methods that will permit further study of the individual enzymic reactions involved in the intrahepatic conjugation of bile acids with amino acids.
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?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. J. Mihalik, S. J. Steinberg, Z. Pei, J. Park, D. G. Kim, A. K. Heinzer, G. Dacremont, R. J. A. Wanders, D. A. Cuebas, K. D. Smith, et al.
Participation of Two Members of the Very Long-chain Acyl-CoA Synthetase Family in Bile Acid Synthesis and Recycling
J. Biol. Chem., June 28, 2002; 277(27): 24771 - 24779.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
K. Solaas, A. Ulvestad, O. Söreide, and B. F. Kase
Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts
J. Lipid Res., July 1, 2000; 41(7): 1154 - 1162.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
S. J. Steinberg, S. J. Mihalik, D. G. Kim, D. A. Cuebas, and P. A. Watkins
The Human Liver-specific Homolog of Very Long-chain Acyl-CoA Synthetase Is Cholate:CoA Ligase
J. Biol. Chem., May 19, 2000; 275(21): 15605 - 15608.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1978 by the American Society for Biochemistry and Molecular Biology.