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Study of a Hydrophobic Protein Fraction Isolated from Milk Proteose-Peptone

Applied Biochemistry Laboratory, Associated with INRA, Faculty of Sciences, University of Nancy 1, BP 239, 54506 Vandoeuvre les Nancy, France

ABSTRACT

Hydrophobic interaction chromatography was used to isolate a hydrophobic fraction from proteose-peptone. Further fractionations by means of gel permeation chromatography and SDS-PAGE led to determining four protein groups. Group 2 containing principally component 3 was especially investigated. Electrophoretic analysis resulted in two major polypeptides with apparent molecular weights of 17,000 and 7000; the largest reacting as a glycoprotein is thought to be an anti-milk fat globule membrane-reacting protein.

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