作者: Keith Brew , Francis J. Castellino , Thomas C. Vanaman , Robert L. Hill
DOI: 10.1016/S0021-9258(19)63827-5
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摘要: The complete amino acid sequence of bovine α-lactalbumin has been established. unique was deduced by characterization the tryptic, chymotryptic, and peptic peptides isolated from enzymic hydrolysates two fragments obtained on cleavage S-aminoethyl-α-lactalbumin with cyanogen bromide as described earlier. Important overlapping were also analysis chymotryptic unmodified or S-carboxymethyl-α-lactalbumin. Bovine contains 123 residues NH2-terminal glutamic COOH-terminal leucine. In accord earlier reports, a considerable similarity in to hen egg-white lysozyme. Alignment sequences these proteins shows that 49 are identical an additional 23 conservative replacements.