TY - JOUR
T1 - 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
AU - Muramoto, Koji
AU - Sunahara, Satoshi
AU - Kamiya, Hisao
PY - 1987/1/1
Y1 - 1987/1/1
N2 - 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.
AB - 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.
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U2 - 10.1080/00021369.1987.10868227
DO - 10.1080/00021369.1987.10868227
M3 - Article
AN - SCOPUS:84954871456
VL - 51
SP - 1607
EP - 1616
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 6
ER -