The primary structure of alpha-lactalbumin from camel milk.
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.
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002162:Camelus / Q000378:metabolism*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D006041:Goats; D006168:Guinea Pigs; D006801:Humans; D006868:Hydrolysis; D007768:Lactalbumin / Q000302:isolation & purification; D007614:Macropodidae; D008892:Milk / Q000032:analysis*; D011817:Rabbits; D051381:Rats; D013045:Species Specificity
D007768:Lactalbumin