Verification of protein disulfide bond arrangement by in‐gel tryptic digestion under entirely neutral pH conditions | Zendy

Saito Kazuki | Zendy; Yasuo Itsuki | Zendy; Uchimura Hiromasa | Zendy; KoideYoshida Shizuyo | Zendy; Mizuguchi Takaaki | Zendy; Kiso Yoshiaki | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research