The primary structure of α‐lactalbumin from camel milk

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Abstract
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 [kilodalton]. 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.