title: Partial purification of the apolipoprotein E receptor of rat liver membrane.
abstract: The liver has two distinct lipoprotein receptors; one is the apolipoprotein (apo) B, E receptor and the other the apo-E receptor. In this study, the protein to which apo-E HDLc (cholesterol-induced high density lipoprotein containing apo-E as the predominant protein species) bound specifically was partially purified from the rat liver membrane by ion exchange chromatography and preparative gel electrophoresis. The molecular weight of the protein was estimated to be about 36K daltons and the protein bound to 125I-apo-E HDLc in a specific and saturable manner, suggesting that the protein is the apo-E receptor.
authors.forename: M
authors.initials: M
authors.lastname: Kinoshita
authors.forename: T
authors.initials: T
authors.lastname: Teramoto
authors.forename: H
authors.initials: H
authors.lastname: Kato
authors.forename: Y
authors.initials: Y
authors.lastname: Hashimoto
authors.forename: C
authors.initials: C
authors.lastname: Naito
authors.forename: G
authors.initials: G
authors.lastname: Toda
authors.forename: H
authors.initials: H
authors.lastname: Oka
mesh_terms: D000818:Animals; D008099:Liver / Q000032:analysis*; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D008297:Male; D008566:Membranes / Q000032:analysis; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000302:isolation & purification*
chemical_list: D026503:Low Density Lipoprotein Receptor-Related Protein-1; D011956:Receptors, Cell Surface