منابع مشابه
Hog Intrinsic Factor I. ISOLATION OF VITAMIN Bn-BINDING FRACTIONS FROM HOG PYLORUS”
Intrinsic factor and another high capacity vitamin Blzbinding protein devoid of intrinsic factor activity were isolated from hog pyloric mucosa. Both components were isolated as their vitamin Blz complexes and in noncomplexed form. All four preparations are glycoproteins and appear to be homogeneous as judged by starch gel electrophoresis, velocity sedimentation analysis, column chromatography,...
متن کاملHog intrinsic factor. I. Isolation of vitamin B12-binding fractions from hog pylorus.
Intrinsic factor and another high capacity vitamin Blzbinding protein devoid of intrinsic factor activity were isolated from hog pyloric mucosa. Both components were isolated as their vitamin Blz complexes and in noncomplexed form. All four preparations are glycoproteins and appear to be homogeneous as judged by starch gel electrophoresis, velocity sedimentation analysis, column chromatography,...
متن کاملBlocking of hog intrinsic factor by human gastric juice and certain mucopolysaccharides, including blood group substance.
Intrinsic factor can bind vitamin B12 and simultaneously attach to receptors on liver or small intestine in a calcium-dependent manner (1). There appears to be a stoichiometric relationship between the receptors, intrinsic factor and vitamin B12 (2). This report, previously presented in preliminary form (3), is concerned with blocking of the receptor sites for hog intrinsic factor by human gast...
متن کاملBlocking of Hog Intrinsic Factor by Human Gastric Juice and Certain Mucopolysaccharides , in - Cluding Blood
Intrinsic factor can bind vitamin B12 and simultaneously attach to receptors on liver or small intestine in a calcium-dependent manner (1). There appears to be a stoichiometric relationship between the receptors, intrinsic factor and vitamin B12 (2). This report, previously presented in preliminary form (3), is concerned with blocking of the receptor sites for hog intrinsic factor by human gast...
متن کاملStudies on the mechanism of cobalamin binding to hog intrinsic factor.
Cobalamin binding to hog intrinsic factor has been studied by affinity chromatography, and the cobalt atom of the cobalamin tested was found to be no more than 5 A from the surface of the protein. A comparative study of the binding of the c carboxylic acid derivative versus the c amide at C, of the B-pyrrole ring indicates that a change in charge at this position of the corrin ring has little e...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1967
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96224-1