Future trends in milk consumption and composition.
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Biomedical subjects
Publications and source records attributed to G C Cheeseman.
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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.
The molecular weights of milk-fat-globule-membrane proteins solubilized in sodium dodecyl sulphate were estimated by gradient gel electrophoresis. Standard curves were calibrated from both protein and glycoprotein markers of known molecular weight. Six major proteins were observed with Coomassie Blue staining and six with periodic acid-Schiff staining. The behaviour of the membrane proteins and the marker proteins was compared on several different single strength sodium dodecyl sulphate-polyacrylamide gels between 3 and 12% (w/v). The results were used to calculate the free electrophoretic mobility and retardation coefficient of each protein. Glycoprotein markers had a significantly lower mean free electrophoretic-mobility value than the protein markers. Three of the milk-fat-globule-membrane glycoproteins were shown to be independent of any of the Coomassie Blue-stained bands. On the basis of a comparison of the free electrophoretic-mobility and retardation- coefficient values of markers and unknown proteins the most appropriate standard curve for molecular-weight estimation was chosen.
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