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.

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The addition of phenol (about 1 %) to 6 M HCl largely prevented destruction of tryptophan during hydrolysis of peptides at 110°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 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.

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詳細情報 詳細情報について

  • CRID
    1390282681441844736
  • NII論文ID
    130000025042
  • DOI
    10.1271/bbb1961.51.1607
  • COI
    1:CAS:528:DyaL2sXkslemu78%3D
  • ISSN
    18811280
    00021369
    http://id.crossref.org/issn/00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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