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PMID: 1138918 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Isolation and partial characterization of intestinal calcium-binding proteins from the cow, pig, horse, guinea pig, and chick.

Biochimica et biophysica acta ·Vol. 393 ·No. 1 ·1975-05-30 ·Pages 134-42

Fullmer CS, Wasserman RH

Abstract

1. Intestinal calcium-binding proteins have been isolated in high purity from mucosal tissue of the cow, pig, horse, guinea pig, and chick. The proteins from all species exhibit rapid, although not identical, electrophoretic mobilities and possesses high affinities for calcium. 2. The intestinal calcium-binding proteins of mammalian origin exhibit a molecular size of approx. 11 000 by calibrated gel filtration and 9000 on the basis of amino acid composition. The analogous chick protein was found to be about 27 000-28 000 molecular weight by these methods. 3. The amino acid composition of each intestinal calcium-binding protein has been determined and indicates a considerable degree of similarity, especially among the mammalian species. 4. Immunoassay procedures have failed to show any species cross-reactivity when tested against antiserum prepared in response to either the bovine or chick intestinal calcium-binding protein.

MeSH Terms
Amino Acids/analysis Animals Binding Sites Calcium/metabolism Cattle Chickens Chromatography, Gel Electrophoresis, Disc Guinea Pigs Horses Intestinal Mucosa/analysis,metabolism Intestine, Small/analysis,metabolism Protein Binding Proteins/isolation & purification,metabolism Receptors, Drug Species Specificity Spectrophotometry, Ultraviolet Swine
Chemicals
Amino Acids Proteins Receptors, Drug Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fullmer C S
Wasserman R H
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-05-30
Pages
134-42
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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