The amino acid sequence of Lady Amherst's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes.
The amino acids of Lady Amherst's pheasant and golden pheasant egg-white lysozymes have been sequenced. The carboxymethylated lysozymes were digested with trypsin followed by sequencing of the tryptic peptides. Lady Amherst's pheasant lysozyme proved to consist of 129 amino acid residues, and a relative molecular mass of 14,423 Da was calculated. This lysozyme had 6 amino acids substitutions when compared with hen egg-white lysozyme: Phe3 to Tyr, His15 to Leu, Gln41 to His, Asn77 to His, Gln 121 to Asn, and a newly found substitution of Ile124 to Thr. The amino acid sequence of golden pheasant lysozyme was identical to that of Lady Amherst's phesant lysozyme. The phylogenetic tree constructured by the comparison of amino acid sequences of phasianoid birds lysozymes revealed a minimum genetic distance between these pheasants and the turkey-peafowl group.
Araki
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Laboratory of Biochemistry, Faculty of Agriculture, Kyushu Tokai University, Kumamoto, Japan.
Kuramoto
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Torikata
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D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010802:Phylogeny; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D009113:Muramidase