Profiling of genetic variants of bovine kappa-casein macropeptide
1997
Coolbear, K.P. | Elgar, D.F. | Ayers, J.S. (Massey Univ., Palmerston North (New Zealand). Dept. of Chemistry)
Bovine kappa-caseins of single variant phenotype (AA and BB) were purified from milk and the corresponding kappa-casein macropeptides prepared by chymosin hydrolysis. The macropeptides were characterized by PAGE, Mono Q- and reverse-phase HPLC. Chromatographic profiles showed marked differences between the monovariant macropeptides, attributable to differences in glycosylation. The B variant macropeptide was found to be more highly glycosylated than the A variant, with an apparently greater number of oligosaccharide chains per peptide and a higher level of sialylation.
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