Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins. |
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| Authors: | A B Kosek D Durbin A Jonas |
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| Affiliation: | Department of Biochemistry, University of Illinois, College of Medicine at Urbana-Champaign, 506 South Mathews Avenue, Urbana, Illinois, 61801, USA. |
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| 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
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