Beg O U, von Bahr-Lindström H, Zaidi Z H, Jörnvall H
Eur J Biochem. 1985 Mar 1;147(2):233-9. doi: 10.1111/j.1432-1033.1985.tb08741.x.
The primary structure of camel alpha-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 alpha-lactalbumin has 123 residues and a molecular mass of 14.6 kDa. The amino acid sequence is strictly homologous to alpha-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 alpha-lactalbumins with characterized structures. All residues ascribed critical structural or functional roles are strictly invariant in the camel protein.