Disulphide arrangement in bovine caseins: localization of intrachain disulphide bridges in monomers of κ- and αs2-casein from bovine milk
- 1 November 1994
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 61 (4) , 485-493
- https://doi.org/10.1017/s0022029900028417
Abstract
Naturally occurring monomeric κ-casein and αs2-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.Keywords
This publication has 25 references indexed in Scilit:
- The multimeric structure and disulfide‐bonding pattern of bovine κ‐caseinEuropean Journal of Biochemistry, 1992
- Localization of two interchain disulfide bridges in dimers of bovine αs2‐caseinEuropean Journal of Biochemistry, 1992
- Purification of disulphide-linked αs2- and κ-casein from bovine milkJournal of Dairy Research, 1991
- Strategies for determination of disulphide bridges in proteins using plasma desorption mass spectrometryJournal of Mass Spectrometry, 1990
- Ion-exchange fast protein liquid chromatography: optimization of the purification of caseins using a non-denaturing detergentJournal of Dairy Research, 1990
- Optimization of sample preparation for plasma desorption mass spectrometry of peptides and proteins using a nitrocellulose matrixJournal of Mass Spectrometry, 1988
- Analysis by fast protein liquid chromatography of variants of κ-casein and their relevance to micellar structure and rennetingJournal of Dairy Research, 1986
- Complete amino acid sequence of bovine αS2‐caseinFEBS Letters, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Micelle-forming characteristics of monomeric and covalent polymeric .kappa.-caseinsBiochemistry, 1970