Publication | Open Access
Lipoprotein binding to canine hepatic membranes. Metabolically distinct apo-E and apo-B,E receptors.
386
Citations
48
References
1981
Year
Adult Dog LiversProteinlipid InteractionLipid PeroxidationLow DensityE ReceptorsHepatotoxicityMetabolic SignalingHepatic MembranesHealth SciencesOxysterolBiochemistryLiver PhysiologyPharmacologySignal TransductionHepatologySites.the Binding SitePhysiologyLipoprotein MetabolismMedicineLipid Synthesis
Hepatic membranes from adult dog livers have receptors which bind to lipoproteins containing the E apoprotein (the apo-E HDL,) but lack specific receptors for the apo-B-containing low density lipoproteins (LDL).Scatchard analysis of direct binding data for '251-apo-E HDL, revealed nonlinearity of the binding which could be resolved into two components, suggesting the presence of two separate binding sites.The binding site for apo-E HDL, that possessed the highest affinity ( K d = ' The abbreviations used are: apo, apoprotein; LDL, low density lipoproteins; HDL, high density lipoproteins ( d = 1.125-1.21);apo-E HDL,, cholesterol-induced plasma lipoproteins that contain the E apoprotein as the only protein constituent, are cholesteryl ester rich, and float at a lower density ( d = 1.006-1.02);K,,, equilibrium dissociation constant.
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