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Isolation, preparation and the amino acid composition of 4 milk-fat globule membrane proteins solubilized by treatment with sodium dodecyl sulphate

Published online by Cambridge University Press:  01 June 2009

T. E. Cawston ,
M. Anderson  and
G. C. Cheeseman
T. E. Cawston
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
M. Anderson
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
G. C. Cheeseman
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
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Summary

Milk-fat globule membrane (MFGM) proteins were solubilized by treatment with SDS. Four of the major proteins were isolated as SDS complexes using column chromatography. The purity of each isolate was determined by SDS polyacrylamide gel electrophoresis and sufficient of each protein was obtained for amino acid analysis. The amino acid compositions of the isolated MFGM proteins and a total MFGM protein extract were determined. Differences in amino acid composition were found in particular between the major MFGM glycoprotein and the other 3 membrane proteins. The relationships of the amino acid composition to protein properties and structure are discussed.

Type
Original Articles
Information
Journal of Dairy Research , Volume 43 , Issue 3 , October 1976 , pp. 401 - 409
Copyright
Copyright © Proprietors of Journal of Dairy Research 1976

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