HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jonas, A. Search for Related Content PubMed PubMed Citation Articles by Jonas, A. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol 27, 689-698, Copyright © 1986 by Lipid Research, Inc.

REVIEWS

Synthetic substrates of lecithin: cholesterol acyltransferase

A Jonas

Investigation of the substrate specificity of lecithin: cholesterol acyltransferase has been greatly aided by the use of synthetic particles containing the molecular lipid substrates and the apolipoprotein activators of the enzyme. These synthetic particles, in vesicle or disc-like micelle form, are described in some detail noting their preparation, properties, advantages, and limitations as substrates for lecithin:cholesterol acyltransferase. The reactions of the enzyme with the synthetic particles are reviewed in terms of acyl donor and acceptor specificity, activation by apolipoproteins, effects of various inhibitors, and the kinetics of the reaction.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				P. V. Subbaiah, J. M. Sowa, and M. H. Davidson Evidence for altered positional specificity of LCAT in vivo: studies with docosahexaenoic acid feeding in humans J. Lipid Res., December 1, 2004; 45(12): 2245 - 2251. [Abstract] [Full Text] [PDF]

				A. Hockerstedt, M. J. Tikkanen, and M. Jauhiainen LCAT facilitates transacylation of 17{beta}-estradiol in the presence of HDL3 subfraction J. Lipid Res., March 1, 2002; 43(3): 392 - 397. [Abstract] [Full Text] [PDF]

				B. Vanloo, F. Peelman, K. Deschuymere, J. Taveirne, A. Verhee, C. Gouyette, C. Labeur, J. Vandekerckhove, J. Tavernier, and M. Rosseneu Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease J. Lipid Res., May 1, 2000; 41(5): 752 - 761. [Abstract] [Full Text]

				G. W. Buchko, W. D. Treleaven, S. J. Dunne, A. S. Tracey, and R. J. Cushley Structural Studies of a Peptide Activator of Human Lecithin-Cholesterol Acyltransferase J. Biol. Chem., February 9, 1996; 271(6): 3039 - 3045. [Abstract] [Full Text] [PDF]