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 journalArticlepeer-review

    33 Citations (Scopus)

    Abstract

    The addition of phenol (about 1 % to 6 M HCl largely prevented destruction of tryptophan during hydrolysis of pep tides at 1l0°C for 22hr. Tryptophan recovery depended on the volume of 6 M HCl 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 high performance 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)

    Fingerprint

    Dive into the research topics of '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'. Together they form a unique fingerprint.

    Cite this