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Isolation and characterization of a major glycoprotein from milk-fat-globule membrane of human breast milk.

Authors
  • Imam, A
  • Laurence, D J
  • Neville, A M
Type
Published Article
Journal
The Biochemical journal
Publication Date
Jan 01, 1981
Volume
193
Issue
1
Pages
47–54
Identifiers
PMID: 7305935
Source
Medline
License
Unknown

Abstract

A major periodate--Schiff-positive component from milk-fat-globule membrane of human breast milk has been purified by selectively extracting the membrane glycoproteins, followed by lectin affinity chromatography and gel filtration on Sephadex G-200 in the presence of protein-dissociating agents. The purified glycoprotein, termed epithelial membrane glycoprotein (EMGP-70), has an estimated mol.wt. of 70 000 and yields a single band under reducing conditions on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The glycoprotein contains 13.5% carbohydrate by weight, with fucose, mannose, galactose, N-acetylglucosamine and sialic acid 17.2, 17.0, 21.1, 7.9 and 36.6% respectively of the carbohydrate moiety. Aspartic and glutamic acid and serine are the major amino acid residues.

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