Disulphide arrangement in bovine caseins: localization of intrachain disulphide bridges in monomers of kappa- and alpha s2-casein from bovine milk.
Naturally occurring monomeric kappa-casein and alpha s2-casein in bovine milk were purified by ion-exchange chromatography in order to localize potential intrachain disulphide bridges. Enzymic cleavage of the proteins followed by mass spectrometry and amino acid sequence analysis of cystine-containing peptides revealed the presence of an intrachain disulphide bond in both proteins.
Rasmussen
L K
LK
Protein Chemistry Laboratory, University of Aarhus, Denmark.
Højrup
P
P
Petersen
T E
TE
D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000737:chemistry* / Q000302:isolation & purification; D002417:Cattle; D004220:Disulfides / Q000032:analysis*; D005260:Female; D013058:Mass Spectrometry / Q000662:veterinary; D008892:Milk / Q000737:chemistry*; D008969:Molecular Sequence Data
D002364:Caseins; D004220:Disulfides