The multimeric structure and disulfide-bonding pattern of bovine kappa-casein.
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.
Rasmussen
L K
LK
MD Foods Research and Development Center, Brabrand, Denmark.
Højrup
P
P
Petersen
T E
TE
D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000737:chemistry* / Q000235:genetics; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011487:Protein Conformation
D002364:Caseins; D004220:Disulfides; D046911:Macromolecular Substances; D010446:Peptide Fragments