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Verification of protein disulfide bond arrangement by in‐gel tryptic digestion under entirely neutral pH conditions
Author(s) -
Saito Kazuki,
Yasuo Itsuki,
Uchimura Hiromasa,
KoideYoshida Shizuyo,
Mizuguchi Takaaki,
Kiso Yoshiaki
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900056
Subject(s) - disulfide bond , trypsin , chemistry , digestion (alchemy) , protein disulfide isomerase , chromatography , proteolytic enzymes , proteomics , biochemistry , enzyme , gene
To develop a concise proteomic procedure to verify the protein disulfide bond arrangement, non‐reductive trypsin digestion of neuregulin 1‐β1 (176–246), a model disulfide‐containing protein, was assessed by a proteolytic 18 O‐labeling analysis. As a result, the commonly used in‐gel tryptic digestion method has been improved for use entirely under neutral pH conditions. With this procedure, the disulfide arrangement of proteins could represent a clinical index candidate in pathological proteomic studies.