Modified electrophoretic and digestion conditions allow a simplified mass spectrometric evaluation of disulfide bonds
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F09%3A00207255" target="_blank" >RIV/00216208:11320/09:00207255 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/09:00337531 RIV/00216208:11310/09:10000349 RIV/61989592:15310/09:00010451
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Modified electrophoretic and digestion conditions allow a simplified mass spectrometric evaluation of disulfide bonds
Original language description
Proper formation of disulfide bonds in proteins is a prerequisite to their stability and function. Information on disulfide pattern may therefore serve as an indication of the proper folding of recombinant proteins, and can also be used in protein homology modeling for the purpose of structure refinement. Protein handling and digestion at basic PH leads to disulfide bond scrambling. Here, we present a complete sample handling protocol, which allows processing of disulfide containing proteins at basic PH. We modified the standard SIDS gel electrophoresis and protein digestion conditions by the addition of an oxidative agent, cystamine. This modification prevented disulfide scrambling, which we otherwise observed in the samples handled according to the general protocol. Lysozyme from hen egg was used as a model protein for the development of the method.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Mass Spectrometry
ISSN
1076-5174
e-ISSN
—
Volume of the periodical
44
Issue of the periodical within the volume
11
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
—
UT code for WoS article
000272150300004
EID of the result in the Scopus database
—