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The primary structure of α-lactalbumin from camel milk
Article first published online: 3 MAR 2005
DOI: 10.1111/j.1432-1033.1985.tb08741.x
1742-4658/asset/cover.gif?v=1&s=fc98a9fc84ccc5e1b83463cabb40f397544364eb "European Journal of Biochemistry")
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How to Cite
BEG, O. U., von BAHR-LINDSTRÖM, H., ZAIDI, Z. H. and JÖRNVALL, H. (1985), The primary structure of α-lactalbumin from camel milk. European Journal of Biochemistry, 147: 233–239. doi: 10.1111/j.1432-1033.1985.tb08741.x
Publication History
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received August 27/October 26, 1984) – EJB 84 0939
- Abstract
- Article
- References
- Cited By
The primary structure of camel α-lactalbumin was determined by analysis of the intact protein, and of CNBr fragments and enzymatic peptides from the carboxymethylated protein chain. Results show that camel α-lactalbumin has 123 residues and a molecular mass of 14.6 kDa. The amino acid sequence is strictly homologous to α-lactalbumins characterized, but also exhibits extensive differences: 39 residues differ in relation to the bovine protein and only 35 residues are conserved among hitherto known α-lactalbumins with characterized structures. All residues ascribed critical structural or functional roles are strictly invariant in the camel protein.