Primary structure of rabbit .alpha.-lactalbumin

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Abstract
Rabbit .alpha.-lactalbumin was purified from the milk of New Zealand White rabbits. It existed predominantly as a glycoprotein, containing 5 mol of glucosamine/mol of protein, as well as other sugars. The amino acid sequence of the protein was determined by sequenator analysis and carboxypeptidase digestion. There are 122 amino acids in the protein and a single carbohydrate moiety, probably attached to an asparagine residue at position 45. The C terminus of rabbit .alpha.-lactalbumin is 1 residue shorter than that of the other .alpha.-lactalbumins. Sequence comparisons indicate that the .alpha.-lactalbumin gene was undergoing more frequent mutation than was previously thought. A new method of preparative mapping using 2,5-diphenyloxazole (PPO) fluor to detect peptides is described.