Premium
Sequence determination of a peptide with 55 amino acid residues by Edman degradation and field desorption mass spectrometry
Author(s) -
Katakuse Itsuo,
Matsuo Takekiyo,
Matsuda Hisashi,
Shimonishi Yasutsugu,
Hong YeongMan,
Izumi Yoshiharu
Publication year - 1982
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200090204
Subject(s) - edman degradation , chemistry , chromatography , amino acid , mass spectrometry , peptide sequence , trypsin , peptide , chymotrypsin , molecular mass , lysozyme , biochemistry , enzyme , gene
The amino acid sequence of a polypeptide was determined by a new method combined with field desorption (FD) mass spectrometry and Edman degradation. The polypeptide, N‐terminal BrCN fragment of Streptomyces erythraeus lysozyme with 55 amino acid residues, was cleaved specifically into several peptide fragments by trypsin and chymotrypsin. The molecular weights of subpeptides were determined by FD mass spectrometry. Peptide mixtures were subjected to Edman degradation successively and PTH amino acids released were measured by high performance liquid chromatography. The amino acid sequence was calculated by a computer program from molecular weights of subpeptides and PTH amino acids.