The amino acid sequence of reeves' pheasant (Syrmaticus reevesii) lysozyme.
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.
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu Tokai University, Kumamoto, Japan.
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Araki
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Kuramoto
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Torikata
D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004529:Egg White / Q000032:analysis; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D009113:Muramidase