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Identification of the milk fat globule membrane proteins. I. Isolation and partial characterization of glycoprotein B.

Authors
Type
Published Article
Journal
Biochimica et Biophysica Acta
0006-3002
Publisher
Elsevier
Publication Date
Volume
448
Issue
4
Pages
589–598
Identifiers
PMID: 974148
Source
Medline
License
Unknown

Abstract

The salt soluble proteins from the fat globule membrane of cow's milk were resolved into three fractions by Sephadex column chromatography in sodium dodecyl sulfate. One of the fractions, termed glycoprotein B, was purified by rechromatography to essentially one band on sodium dodecyl sulfate gel electrophoresis. It was found to contain 14% carbohydrate including sialic acid, mannose, galactose, glucose, glucosamine and galactosamine. The amino acid composition of glycoprotein B was determined; it has amino terminal serine and carboxyl terminal leucine. The molecular weight of this glycoprotein as estimated by sodium dodecyl sulfate gel electrophoresis is 49 500.

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