In:
Biochemical Journal, Portland Press Ltd., Vol. 193, No. 1 ( 1981-01-01), p. 47-54
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.
Type of Medium:
Online Resource
ISSN:
0264-6021
Language:
English
Publisher:
Portland Press Ltd.
Publication Date:
1981
detail.hit.zdb_id:
1473095-9
SSG:
12
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