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Partial purification of the apolipoprotein E receptor of rat liver membrane.

Authors: Kinoshita, M  Teramoto, T  Kato, H  Hashimoto, Y  Naito, C  Toda, G  Oka, H 
Citation: Kinoshita M, etal., J Biochem. 1985 Jun;97(6):1803-6.
Pubmed: (View Article at PubMed) PMID:2993274

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.


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CRRD Object Information
CRRD ID: 2302271
Created: 2008-12-08
Species: All species
Last Modified: 2008-12-08
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.