Isolation, preparation and the amino acid composition of 4 milk-fat globule membrane proteins solubilized by treatment with sodium dodecyl sulphate.
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.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008055:Lipids; D008565:Membrane Proteins / Q000302:isolation & purification; D008566:Membranes / Q000032:analysis; D008892:Milk / Q000032:analysis; D008894:Milk Proteins; D012967:Sodium Dodecyl Sulfate; D012995:Solubility
D000596:Amino Acids; D008055:Lipids; D008565:Membrane Proteins; D008894:Milk Proteins; D012967:Sodium Dodecyl Sulfate