Studies on human alpha(s)- and kappa-casein fractions and human caseinoglycomacropeptide |
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| Authors: | Malpress F H Seid-Akhavan M |
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| Affiliation: | Department of Biochemistry, Queen's University, Belfast, N. Ireland. |
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| Abstract: | 1. Fractions have been obtained from human whole casein closely resembling the αs- and κ-fractions of cow casein. 2. The αs-fraction (human αs-casein) is calcium-sensitive, heterogeneous in zone analysis and inert towards rennin. 3. The κ-fraction (human κ-casein) is calcium-insensitive, heterogeneous in zone analysis, and forms a soluble glycopeptide when acted upon by rennin. 4. Human κ-casein stabilizes human αs-casein in the presence of Ca2+ ions. 5. The glycopeptides released by rennin from human casein and from cow casein have been compared. There are important differences in both the peptide and non-peptide structures of the two compounds. 6. In both human and bovine glycopeptides some of the carbohydrate residues are joined to the peptide by O-glycosidic links with threonine, and possibly with serine. |
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