Kosek_1999_Biochem.Biophys.Res.Commun_258_548

Reference

Title : Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins - Kosek_1999_Biochem.Biophys.Res.Commun_258_548
Author(s) : Kosek AB , Durbin D , Jonas A
Ref : Biochemical & Biophysical Research Communications , 258 :548 , 1999
Abstract :

The first step in the reaction of lecithin cholesterol acyltransferase (LCAT) with lipoproteins is the interfacial binding of the enzyme to the lipid surfaces. In this study the equilibrium dissociation constants (Kds) for the interaction of pure human plasma LCAT with LDL, HDL2, HDL3, and a reconstituted discoidal HDL (rHDL) were determined by the activity-inhibition method. In addition, enzyme kinetics were measured with each of the lipoprotein substrates. Based on phospholipid concentrations, the Kd values (0.9 x 10(-5) to 4.6 x 10(-5) M) increased in the order rHDL = HDL3

PubMedSearch : Kosek_1999_Biochem.Biophys.Res.Commun_258_548
PubMedID: 10329423
Gene_locus related to this paper: human-LCAT

Related information

Gene_locus human-LCAT

Citations formats

Kosek AB, Durbin D, Jonas A (1999)
Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins
Biochemical & Biophysical Research Communications 258 :548

Kosek AB, Durbin D, Jonas A (1999)
Biochemical & Biophysical Research Communications 258 :548