PMID: 11902953Mar 21, 2002Paper

Isolation and analysis of kappa-casein glycomacropeptide from goat sweet whey

Journal of Agricultural and Food Chemistry
Eryck R Silva-HernandezLech Ozimek

Abstract

Glycomacropeptide (GMP) was purified from goat sweet whey by anion-exchange and hydrophobic interaction chromatography. Approximately 0.06% (w/v) of sweet whey was recovered as GMP. Amino acid analysis of the GMP preparation showed that the content of phenylalanine (an amino acid that does not occur in goat GMP) was negligible, indicating that the GMP was of high purity. The goat GMP contained 25 microg sialic acid per mg of dry weight. This was approximately 3-fold lower than the sialic acid concentration in bovine GMP reported in the literature. Gel electrophoretic results demonstrated that most of the goat GMP occurs as a dimer. The GMP was intensely stained with Coomassie blue in 50% methanol containing 12.5% (w/v) trichloroacetic acid, but showed very weak metachromasia with the same dye in 45% methanol containing 10% acetic acid, a preparation commonly used to stain protein.

References

Jun 1, 1978·The Journal of Dairy Research·F AddeoB Ribadeau-Dumas
Jan 1, 1994·Journal of Dairy Science·R PuenteP Hueso
Dec 20, 1999·Journal of Agricultural and Food Chemistry·T Nakano, L Ozimek
Mar 10, 2001·The British Journal of Nutrition·E P Brody

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Citations

Mar 9, 2010·The British Journal of Nutrition·Jennifer B KeoghPeter M Clifton
Apr 4, 2009·Journal of Chromatography. a·Rafael A LiraMaria C H da Silva
Jan 29, 2005·Journal of Agricultural and Food Chemistry·Takuo NakanoLech Ozimek

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