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Milk Fat-Globule Membrane as Possible Origin of Proteose-Peptone Glycoproteins^{1 ,2,}

Department of Food Science and Human Nutrition, Michigan State University, East Lansing 48824

ABSTRACT

Affinity chromatography on a Concanavalin A-Sepharose support was used to isolate glycoprotein fractions from proteose-peptone and the soluble protein of the milk fat-globule membrane. The proteose-peptone glycoprotein was shown by compositional and electrophoretic analyses to consist principally of component 3. Immuno-double diffusion experiments indicated at least one antigenetically similar component in the proteosepeptone glycoprotein and the soluble protein of milk fat globule membrane glycoprotein fraction-1. Electrophoretic comparison (sodium dodecyl sulfate — polyacrylamide gel electrophoresis) of these two glycoprotein fractions revealed four protein zones common to both fractions with apparent molecular weights of 18,000 to 21,000, 24,800, 28,200, and 32,200. Immunological techniques identified the 18,000 to 21,000 molecular weight component as the antigenically common species. The fat globule membrane as a possible source of proteose-peptone component 3 is considered.

¹ Michigan Agricultural Experiment Station Journal Article No. 10297.

² Supported in part by a grant from Dairy Research, Inc.

³ Knudsen Corporation.

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