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The amino acid sequence of reeves' pheasant (Syrmaticus reevesii) lysozyme
T Araki1, M Kuramoto, T Torikata
1Laboratory of Biochemistry, Faculty of Agriculture, Kyushu Tokai University, Kumamoto, Japan.
Agricultural and Biological Chemistry
|July 1, 1991
Abstract:
The amino acid sequence of reeves' pheasant lysozyme was analyzed. Carboxymethylated lysozyme was digested with trypsin and resulting peptides were analyzed using the DABITC/PITC double coupling manual Edman method. The established amino acid sequence had seven substitutions, Tyr3, Leu15, His41, His77, Ser79, Arg102, and Asn121, compared with hen egg-white lysozyme. Ser79 was the first found in a bird lysozyme. A substitution in the active site was found in position 102 which has been considered to participate in the substrate binding at subsites A-C.