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A Spectrographic Analysis of Two Protein Fractions of the Fat-Globule Membrane of Normal Cow's Milk

Department of Dairy

S. T. Bass

Department of Agricultural Chemistry, Michigan Agricultural Experiment Station, East Lansing

ABSTRACT

The most closely associated protein materials of the fat-globule membrane of normal cow's milk have been separated into two fractions, based upon their solubility in a 0.02-M sodium chloride solution, subsequent to an ethanol-ethyl ether treatment (3). The ash content of the soluble and insoluble fractions, following exhaustive dialysis against running tap-water and four changes of distilled water over a period of 72 to 96 hours, was 7.06 and 2.08, respectively. These values are considerably higher than corresponding values for other milk proteins. Distribution of minerals between the two protein fractions becomes of academic interest, in view of our observations associating the alkaline phosphomonoesterases with the soluble protein fraction, and xanthine oxidase with the insoluble fraction (3). The ash from these proteins presented an excellent opportunity for a spectrographic analysis of their constituent elements.

The residual ash of the protein samples was dissolved in four milliliters of 1:1 HCl.

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