The hydrophobic nature of the pig intrinsic factor receptor in the intestine.
The pig intestinal intrinsic factors receptor has been isolated and dissociated into its alpha and beta subunits. The beta subunit was found to be more hydrophobic than the alpha subunit. In a detergent solution only the alpha subunit was accessible to digestion with papain. The whole isolated receptor was introduced into artificial single bilayer liposomes where is apparently was randomly oriented. Liposomes containing the receptor were digested with papain and the polypeptide segments that stayed in the lipid fraction were extracted and analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Four species were found with Mr values of 23 000, 45 000, 70 000 and 86 000.
D000818:Animals; D002846:Chromatography, Affinity; D007082:Ileum / Q000378:metabolism*; D007437:Intrinsic Factor / Q000378:metabolism*; D008051:Lipid Bilayers; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000302:isolation & purification* / Q000378:metabolism; D018000:Receptors, Peptide; D013552:Swine
D008051:Lipid Bilayers; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; C028199:intrinsic factor receptor; D007437:Intrinsic Factor