Isolation of monoclonal antibodies monospecific for bovine kappa-casein
- PMID: 2283404
- DOI: 10.3168/jds.S0022-0302(90)78959-X
Isolation of monoclonal antibodies monospecific for bovine kappa-casein
Abstract
Bovine kappa-casein represents a major portion of the total protein present in milk and is required for formation of the caseinate micelles responsible for the transportation of both calcium and phosphorous. Two monoclonal antibodies directed against bovine kappa-casein have been isolated. Both monoclonal antibodies are highly specific for bovine kappa-casein. Western analysis of denatured kappa-casein suggests epitope specificity is, in part, conformationally dependent. Additional epitope mapping with chymosin and neuraminidase also suggest antibody binding is in the region of the amino acid sequence Pro-Thr-Thr at positions 92 to 94 and 134 to 136.
Similar articles
-
Isolation and characterization of monoclonal antibodies monospecific for bovine alpha-casein and beta-casein.J Dairy Sci. 1991 Mar;74(3):803-10. doi: 10.3168/jds.S0022-0302(91)78228-3. J Dairy Sci. 1991. PMID: 1712797
-
Isolation and characterization of monoclonal antibody directed against bovine alpha s2-casein.J Dairy Sci. 1991 Sep;74(9):2872-8. doi: 10.3168/jds.S0022-0302(91)78468-3. J Dairy Sci. 1991. PMID: 1723415
-
Epitope characterization of a supramolecular protein assembly with a collection of monoclonal antibodies: the case of casein micelle.Mol Immunol. 2009 Mar;46(6):1058-66. doi: 10.1016/j.molimm.2008.09.028. Epub 2008 Nov 6. Mol Immunol. 2009. PMID: 18992943
-
Micelle stability: kappa-casein structure and function.J Dairy Sci. 1998 Nov;81(11):3004-12. doi: 10.3168/jds.S0022-0302(98)75864-3. J Dairy Sci. 1998. PMID: 9839241 Review.
-
Caseins of various origins and biologically active casein peptides and oligosaccharides: structural and physiological aspects.Mol Cell Biochem. 1989 May 4;87(1):5-30. doi: 10.1007/BF00421079. Mol Cell Biochem. 1989. PMID: 2671666 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources