Measurement of Tryptophan in Peptides by Acid Hydrolysis in the Presence of Phenol and its Application to the Amino Acid Sequence of a Sea Anemone Toxin

Koji Muramoto, Satoshi Sunahara, Hisao Kamiya

    Research output: Contribution to journalArticle

    2 Citations (Scopus)

    Abstract

    The addition of phenol (about 1%) to 6 m HC1 largely prevented destruction of tryptophan during hydrolysis of peptides at 110°C for 22 hr. Tryptophan recovery depended on the volume of 6 m HC1 containing phenol and the concentration of phenol. The maximum tryptophan recovery was 85% for a standard amino acid mixture. The recovery was slightly lower for proteins. This hydrolytic procedure was advantageous for micro amino acid analysis using a conventional highperformance liquid chromatography with a precolumn labeling technique. The method was used in the amino acid sequence analysis of a minor component of sea anemone toxins isolated from Anthopleura fuscoviridis. The toxin consisted of 48 amino acid residues with three tryptophan residues.

    Original languageEnglish
    Pages (from-to)1607-1616
    Number of pages10
    JournalAgricultural and Biological Chemistry
    Volume51
    Issue number6
    DOIs
    Publication statusPublished - 1987 Jan 1

    ASJC Scopus subject areas

    • Biochemistry, Genetics and Molecular Biology(all)
    • Agricultural and Biological Sciences(all)

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