Open AccessThe multimeric structure and disulfide‐bonding pattern of bovine κ‐casein
Author(s) -
RASMUSSEN Lone K.,
HØJRUP Peter,
PETERSEN Torben E.
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb17040.x
Subject(s) - disulfide bond , casein , monomer , chemistry , protein subunit , sequence (biology) , crystallography , biochemistry , stereochemistry , chromatography , organic chemistry , polymer , gene
Bovine κ‐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 κ‐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 [ 14 C]carboxymethylated and untreated bulk milk, as well as a milk sample from a κ‐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.