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• W2008049853 abstract "We have investigated the binding of human apolipoprotein A-IV (apo A-IV) to human hepatocellular plasma membranes. Addition of increasing concentrations of radiolabeled apo A-IV to hepatic plasma membranes, in the presence and absence of a 25-fold excess of unlabeled apo A-IV, revealed saturation binding to the membranes with a KD of 154 nM and a binding maximum of 1.6 ng/microgram of membrane protein. The binding was temperature-insensitive, partially calcium-dependent, abolished when apo A-IV was denatured by guanidine hydrochloride or when the membranes were treated with Pronase and decreased when apo A-IV was incorporated into phospholipid/cholesterol proteoliposomes. In displacement studies using purified apolipoproteins and isolated lipoproteins, only unlabeled apo A-IV, apo A-I and high-density lipoproteins effectively competed with radiolabeled apo A-IV for membrane binding sites. We conclude that human apo A-IV exhibits high-affinity binding to isolated human hepatocellular plasma membranes which is saturable, reversible and specific." @default.
• W2008049853 created "2016-06-24" @default.
• W2008049853 creator A5017431147 @default.
• W2008049853 creator A5062615822 @default.
• W2008049853 date "1990-05-01" @default.
• W2008049853 modified "2023-10-16" @default.
• W2008049853 title "Binding of human apolipoprotein A-IV to human hepatocellular plasma membranes" @default.
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• W2008049853 doi "https://doi.org/10.1016/0005-2760(90)90311-k" @default.
• W2008049853 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2344444" @default.
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