The multimeric structure and disulfide-bonding pattern of bovine kappa-casein.
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Rasmussen LK, Hojrup P, Petersen TE
The multimeric structure and disulfide-bonding pattern of bovine kappa-casein.
Eur J Biochem. 1992 Jul 1;207(1):215-22. doi: 10.1111/j.1432-1033.1992.tb17040.x.
- PubMed ID
- 1628650 [ View in PubMed]
- Abstract
Bovine kappa-casein was analyzed by SDS/PAGE, MS and amino acid sequence analysis in order to determine its multimeric composition and disulfide-bonding pattern. SDS/PAGE revealed that kappa-casein in the native state can range in size from a monomer to a multimeric structure larger than a decamer. Three types of interchain disulfide linkage, Cys11-Cys11, Cys11-Cys88 and Cys88-Cys88, were all assigned in multimers purified from [14C]carboxymethylated and untreated bulk milk, as well as a milk sample from a kappa-casein-variant-B homozygote Co20. These results indicate that multimerization occurs in a random or at present unpredictable disulfide-bonding pattern regardless of the size of the multimer or the genotype.