THE MULTIMERIC STRUCTURE AND DISULFIDE-BONDING PATTERN OF BOVINE KAPPA-CASEIN

被引：94

作者：

RASMUSSEN, LK

HOJRUP, P

PETERSEN, TE

机构：

[1] AARHUS UNIV,DEPT MOLEC BIOL,DK-8000 AARHUS,DENMARK

[2] ODENSE UNIV,DEPT MOLEC BIOL,DK-5230 ODENSE,DENMARK

[3] MD FOODS RES & DEV CTR,BRABRAND,DENMARK

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 207卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17040.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 [C-14]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.

引用

页码：215 / 222

页数：8

共 41 条

[1] ISOLATION AND CHARACTERIZATION OF THE BOVINE KAPPA-CASEIN GENE [J].