Publication | Open Access
Studies on human αs- and κ-casein fractions and human caseinoglycomacropeptide
40
Citations
25
References
1966
Year
Protein ChemistryMolecular PharmacologyCow CaseinBiochemistryκ-Casein FractionsMedicineBioanalysisImmunologyGlycobiologyHuman Whole CaseinPeptide SciencePharmacologyHuman CaseinCarbohydrate-protein InteractionMolecular MedicineGlycosylation
1. Fractions have been obtained from human whole casein closely resembling the alpha(s)- and kappa-fractions of cow casein. 2. The alpha(s)-fraction (human alpha(s)-casein) is calcium-sensitive, heterogeneous in zone analysis and inert towards rennin. 3. The kappa-fraction (human kappa-casein) is calcium-insensitive, heterogeneous in zone analysis, and forms a soluble glycopeptide when acted upon by rennin. 4. Human kappa-casein stabilizes human alpha(s)-casein in the presence of Ca(2+) 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.
| Year | Citations | |
|---|---|---|
1959 | 6.4K | |
1950 | 3.8K | |
1954 | 3K | |
1963 | 2.6K | |
1957 | 1.8K | |
1955 | 1.1K | |
1955 | 936 | |
1955 | 633 | |
1954 | 575 | |
1961 | 230 |
Page 1
Page 1