Verification of protein disulfide bond arrangement by in-gel tryptic digestion under entirely neutral pH conditions-Reference-Cited by-同舟云学术

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

Published:2010-02-01 Issue:7 Volume:10 Page:1505-1509
ISSN:1615-9853
Container-title:PROTEOMICS
language:en
Short-container-title:Proteomics

Author:

Saito Kazuki,Yasuo Itsuki,Uchimura Hiromasa,Koide-Yoshida Shizuyo,Mizuguchi Takaaki,Kiso Yoshiaki

Funder

Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan

Suntory Institute for Bioorganic Research

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pmic.200900056/fullpdf

Reference13 articles.

1. Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase;Mononen;Proc. Natl. Acad. Sci. USA,1991

2. Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with β2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells;Waheed;Proc. Natl. Acad. Sci. USA,1997

3. A missense mutation encoding Cys73Phe in neurophysin II is associated with autosomal dominant neurohypophyseal diabetes insipidus;Santiprabhob;Mol. Genet. Metab.,2002

4. Raman spectroscopic measurement of total sulfhydryl in intact lens as affected by aging and ultraviolet irradiation. Deuterium exchange as a probe for accessible sulfhydryl in living tissue;East;J. Biol. Chem.,1978

5. Inter- and intramolecular disulfide bond formation and related structural changes in the lens proteins. A Raman spectroscopic study in vivo of lens aging;Ozaki;J. Biol. Chem.,1987

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