Two peptides which promoted growth of the genuine hiochi-bacteria were isolated from bactotryptone by column chromatography on Sephadex G-25 followed by paper chromatography using
n-butanol/acetic acid/water and phenol/water as solvents. One of them was composed of valine (2 moles), methionine and glutamic acid. Both N- and C-terminal amino acids of the peptide were valine. The other was composed of alanine (3 moles) and glutamic acid. Both N- and C-terminal amino acids of the peptide were alanine.
The same methods were applied for isolation of peptide from saké; two peptides were obtained. One of them was composed of methionine (2 moles), glutamic acid and glycine. N- and C-terminal amino acid of the peptide were methionine and glycine, respectively. The other was composed of alanine (3 moles), aspartic acid and glycine. Both N- and C-terminal amino acids of the peptide were alanine.
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