title: Isolation of the porcine ileal intrinsic factor receptor by sequential affinity chromatography.
abstract: An extract containing solubilised receptor was passed through four columns containing Sepharose to which had been covalently coupled anti-cobalophilin IgG, vitamin B-12-intrinsic factor, vitamin B-12, and free intrinsic factor, respectively. Following a wash the receptor was eluted with EDTA, then residual Triton X-100 micelles and vitamin B-12-intrinsic factor were removed by Sephadex G-200 filtration. The receptor was purified 84 000-fold, sodium dodecyl sulphate electrophoresis indicated two subunits and gel filtration of its vitamin B-12-inttrinsic factor complex resolved it into two molecular species.
mesh_terms: D000818:Animals; D002352:Carrier Proteins; D002846:Chromatography, Affinity; D007082:Ileum; D007437:Intrinsic Factor; D008970:Molecular Weight; D011955:Receptors, Drug / Q000302:isolation & purification*; D013552:Swine; D014805:Vitamin B 12
chemical_list: D002352:Carrier Proteins; D011955:Receptors, Drug; D007437:Intrinsic Factor; D014805:Vitamin B 12