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 Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jonas, A. Articles by Wilson, E. R. Search for Related Content PubMed PubMed Citation Articles by Jonas, A. Articles by Wilson, E. R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 260, Issue 5, 2757-2762, 03, 1985

Kinetics of lecithin-cholesterol acyltransferase reaction with discoidal complexes of apolipoprotein A-I.phosphatidylcholine.ether phospholipid.cholesterol

A Jonas, JL Daehler and ER Wilson

Discoidal substrates for purified human lecithin-cholesterol acyltransferase were prepared with human apolipoprotein A-I, cholesterol, and egg phosphatidylcholine (PC) or dipalmitoyl PC, including dihexadecyl PC in various proportions as an enzymatically inert dilutor of the interfacial PC substrate. All the complexes, prepared by the sodium cholate dialysis method, were found to be very similar in size, lipid/apolipoprotein stoichiometry, and apolipoprotein spectral properties to the small discoidal complexes without any dihexadecyl PC, described previously (Jonas, A., and Matz, C.E. (1982) Biochemistry 21, 6867-6872; Jonas, A., and McHugh, H. T. (1984) Biochim. Biophys. Acta 794, 361-372). The kinetic results presented in the form of double reciprocal plots of initial velocity against bulk PC or interfacial PC concentration were linear according to the Verger et al. kinetic model (Verger, R., Mieras, M. C. E., and de Haas, G. H. (1973) J. Biol. Chem. 248, 4023-4034) for an initial enzyme binding via an interfacial recognition site followed by interfacial substrate binding and catalysis, in the presence of a competitive interfacial inhibitor. The results indicate, furthermore, that the affinity of the active site for the substrate and inhibitor is quite similar.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. M. Durbin and A. Jonas The Effect of Apolipoprotein A-II on the Structure and Function of Apolipoprotein A-I in a Homogeneous Reconstituted High Density Lipoprotein Particle J. Biol. Chem., December 12, 1997; 272(50): 31333 - 31339. [Abstract] [Full Text] [PDF]

				D. J. Bolin and A. Jonas Sphingomyelin Inhibits the Lecithin-Cholesterol Acyltransferase Reaction with Reconstituted High Density Lipoproteins by Decreasing Enzyme Binding J. Biol. Chem., August 9, 1996; 271(32): 19152 - 19158. [Abstract] [Full Text] [PDF]