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Disulphide arrangement in bovine caseins: localization of intrachain disulphide bridges in monomers of κ- and αs2-casein from bovine milk

Published online by Cambridge University Press:  01 June 2009

Lone K. Rasmussen ,
Peter Højrup  and
Torben E. Petersen
Lone K. Rasmussen
Affiliation:
Protein Chemistry Laboratory, The Science Park, University of Aarhus, DK-8000 Aarhus C, Denmark
Peter Højrup
Affiliation:
Protein Chemistry Laboratory, The Science Park, University of Aarhus, DK-8000 Aarhus C, Denmark
Torben E. Petersen
Affiliation:
Protein Chemistry Laboratory, The Science Park, University of Aarhus, DK-8000 Aarhus C, Denmark
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Summary

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.

Type
Original articles
Information
Journal of Dairy Research , Volume 61 , Issue 4 , November 1994 , pp. 485 - 493
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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