Mayumi Kuramoto

The Amino Acid Sequence of Lysozyme from Kalij Pheasant (Lophura leucomelana) Egg-white

The amino acid sequence of kalij pheasant lysozyme has been analyzed. From the comparison of the tryptic peptide pattern of kalij pheasant lysozyme and maps from other bird lysozymes followed by the sequencing of tryptic peptides, the amino acid sequence of kalij pheasant was found to be: KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKYESNFNTHATNRNTDGSTDYGIL- QINSRWWCNDGKTPGSRNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAW- VAWRNRCKGTDVSVWTRGCRL. This sequence had 9 amino acid substitutions compared with hen egg-white lysozyme. Two of these substitutions, positions 34 and 121, were newly detected in phasianid birds. The protein genealogy of phasianid bird lysozymes showed some discordance with the morphological classification of these birds.

Amino acid sequence of the N-terminal domain of yam (Dioscorea japonica) aerial tuber acidic chitinase. Evidence for the presence of a wheat germ agglutinin domain in matured acidic chitinase from unstressed tuber

The amino acid sequence of the N-terminal domain of acidic chitinase from unstressed aerial tuber was determined and proved the presence of an N-terminal domain in acidic chitinase. The amino acid sequence was determined on a pyroglutamylaminopeptidase-treated N-terminal fragment of V8 protease and on chymotryptic peptides of this fragment. The sequence determined revealed 8 residues deletion and 2 residues insertion as compared with the N-terminal domain of tobacco basic chitinase. The N-terminal domain determined showed a homology of 40% and 52% with the N-terminal domain of tobacco basic chitinase and wheat germ agglutinin, respectively.

Peptide separation by gel filtration high-performance liquid chromatography using a gradient elution system

Peptides were separated by gel filtration high-performance liquid chromatography with gradient elution. Two gradient elution systems were applied: (1) 0 to 20% acetonitrile in 30 mM phosphate buffer, pH 8.0 and (2) 30 mM phosphate buffer, pH 8.0 to water; with the polymer-type gel filtration column we used, excellent separation of tryptic peptides from hen egg-white lysozyme was achieved within 50 min. System 2 was applied to a separation of V8 protease peptide from yam tuber chitinase and yielded two to three times higher amounts of peptides than reversed-phase high-performance liquid chromatography.