J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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 Helgerud, P.
Right arrow Articles by Norum, K. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Helgerud, P.
Right arrow Articles by Norum, K. R.
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, 271-277, Copyright © 1981 by Lipid Research, Inc.

ARTICLES

Acyl-CoA:cholesterol acyltransferase in human small intestine: its activity and some properties of the enzymic reaction

P Helgerud, K Saarem and KR Norum

Esterification of endogenous cholesterol in human small intestinal mucosa by acyl-CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) was studied using [1-14C]oleoyl-CoA as substrate. The reaction was linear for 2 min only. The esterification of cholesterol was stimulated by albumin, but this effect was dependent on the oleoyl-CoA concentration. When the albumin concentration was 5 g/liter, maximal esterification was obtained with 35 microM oleoyl-CoA. The pH optimum was 7.2-7.8. The ACAT specific activity was highest in microsomal preparations from jejunum (0.21 +/- 0.19 (n = 18) nmol cholesteryl oleate . mg microsomal protein-1 . min-1), and lower in proximal duodenum and distal ileum. Whole homogenates of biopsies had about 1/4 of the activity of the corresponding microsomal preparation. Microsomal preparations from jejunum contained acyl-CoA hydrolase (EC 3.1.2.2) which under the prevailing conditions had a maximal activity of 4.4 nmol oleate formed . microsomal protein-1 . min-1. The high activity of intestinal ACAT in man renders it possible that this enzyme plays a role in cholesterol absorption.
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. Lipid Res.Home page
L. B. Nguyen, S. Shefer, G. Salen, G. S. Tint, F. Ruiz, and J. Bullock
Mechanisms for cholesterol homeostasis in rat jejunal mucosa: effects of cholesterol, sitosterol, and lovastatin
J. Lipid Res., February 1, 2001; 42(2): 195 - 200.
[Abstract] [Full Text]

Home page
 J. Nutr.Home page
P. T. Chan, W. P. Fong, Y. L. Cheung, Y. Huang, W. K. K. Ho, and Z.-Y. Chen
Jasmine Green Tea Epicatechins Are Hypolipidemic in Hamsters (Mesocricetus auratus) Fed a High Fat Diet
J. Nutr., June 1, 1999; 129(6): 1094 - 1101.
[Abstract] [Full Text]

Home page
 J. Nutr.Home page
S.-H. Bok, S.-H. Lee, Y.-B. Park, K.-H. Bae, K.-H. Son, T.-S. Jeong, and M.-S. Choi
Plasma and Hepatic Cholesterol and Hepatic Activities of 3-Hydroxy-3-methyl-glutaryl-CoA Reductase and Acyl CoA: Cholesterol Transferase Are Lower in Rats Fed Citrus Peel Extract or a Mixture of Citrus Bioflavonoids
J. Nutr., June 1, 1999; 129(6): 1182 - 1185.
[Abstract] [Full Text]


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.