Verification of protein disulfide bond arrangement by in-gel tryptic digestion under entirely neutral pH conditions.

Abstract

To develop a concise proteomic procedure to verify the protein disulfide bond arrangement, non-reductive trypsin digestion of neuregulin 1-beta1 (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.

DOI: 10.1002/pmic.200900056

Cite this paper

@article{Saito2010VerificationOP, title={Verification of protein disulfide bond arrangement by in-gel tryptic digestion under entirely neutral pH conditions.}, author={Kazuki Saito and Itsuki Yasuo and Hiromasa Uchimura and Shizuyo Koide-Yoshida and Takaaki Mizuguchi and Yoshiaki Kiso}, journal={Proteomics}, year={2010}, volume={10 7}, pages={1505-9} }