Yerima, A. and Safi, A. and Gastin, I. and Michalski, J.-C. and Saunier, M. and Gueant, J.-L. (1996) Purification by cobalamin-Sepharose affinity chromatography and intrinsic factor-binding activity of an extramembrane proteolytic product from pig ileal mucosa. Biochemical Journal, 313 (2). pp. 675-681.

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Abstract

We have purified a cobalamin-binding protein obtained by papain digestion of pig intestine by cobalamin-AH-Sepharose affinity chromatography, with a purification factor of 17300, a yield of 63 and a cobalamin-binding activity of 11260 pmol/mg of protein. The protein contained 3.8 carbohydrate and was O- and N-glycosylated. Its molecular mass was 69 kDa on SDS/PAGE and its isoelectric point was 5.1. It had a binding activity for both 57Cocobalamin and 57Cocobalamin-intrinsic factor in native PAGE autoradiography and it inhibited the binding of intrinsic factor to the intact intestinal receptor with an IC50 of 49.31 nmol/l in a radioisotope assay. In conclusion, the purified protein shared a binding activity for both cobalamin and intrinsic factor-cobalamin complexes and could correspond to the extracellular domain of the ileal intrinsic factor receptor.

Item Type: Article
Uncontrolled Keywords: cobalamin; glycosylated protein; intrinsic factor; papain; sepharose, affinity chromatography; article; binding affinity; ileum mucosa; isoelectric point; isotope labeling; molecular weight; nonhuman; polyacrylamide gel electrophoresis; priority journal; protein binding; protein degradation; protein purification; protein structure; radioassay; receptor binding; swine, Animals; Autoradiography; Chromatography, Affinity; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Hydrolysis; Ileum; Intestinal Mucosa; Intrinsic Factor; Kinetics; Protein Binding; Proteins; Swine; Vitamin B 12, Sus scrofa
Subjects: Biochemistry, Genetics and Molecular Biology
Divisions: SCIENTIFIC PRODUCTION > Biochemistry, Genetics and Molecular Biology
Depositing User: Administrateur Eprints Administrateur Eprints
Last Modified: 31 Jan 2020 15:44
URI: http://eprints.umi.ac.ma/id/eprint/1622

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