title: Solubilization of the pig ileal intrinsic factor receptor with papain treatment and studies on the solubilized receptor.
abstract: The intrinsic factor receptor, known to consist of two subunits alpha and beta, has been solubilized by papain digestion from porcine small intestine. Papain liberates a part of the outermost subunit (alpha) of the receptor. The solubilized part was called papain-alpha. It was purified by affinity chromatography on Sepharose-vitamin B-12-intrinsic factor gel and its molecular dimensions were measured. Its molecular weight measured with SDS-polyacrylamide gel electrophoresis is 45000, its isoelectric point is 4.2 and it binds the cobalamin-intrinsic factor complex in the same way as the whole receptor.
mesh_terms: D000818:Animals; D007082:Ileum / Q000378:metabolism*; D007437:Intrinsic Factor / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D010206:Papain; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D018000:Receptors, Peptide; D012995:Solubility; D013552:Swine
chemical_list: D046911:Macromolecular Substances; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; C028199:intrinsic factor receptor; D007437:Intrinsic Factor; D010206:Papain