Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine kappa-casein.
Article Details
- CitationCopy to clipboard
Pisano A, Packer NH, Redmond JW, Williams KL, Gooley AA
Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine kappa-casein.
Glycobiology. 1994 Dec;4(6):837-44. doi: 10.1093/glycob/4.6.837.
- PubMed ID
- 7734846 [ View in PubMed]
- Abstract
kappa-Casein is the major glycoprotein in bovine milk. It has a proteinase-sensitive (chymosin) site which cleaves the glycoprotein into two segments: N-terminal para-kappa-casein domain and the C-terminal kappa-casein macroglycopeptide domain which is highly heterogeneous in oligosaccharide content. We have identified six sites of O-glycosylation on the macroglycopeptide by solid-phase Edman degradation: Thr121, Thr131, Thr133, Thr136 (A variant only), Thr142 and Thr165. No Ser residues are glycosylated. The glycosylation status of 15 of 17 potential O-glycosylation sites in the B variant was accurately predicted using the four peptide motifis previously proposed for the glycosylation of human glycophorin A (Pisano, A., Redmond, J.W., Williams, K.L. and Gooley, A.A., Glycobiology, 3, 429-435, 1993), provided one additional assumption is made concerning an inhibitory role for a nearby Ile.