Arg-C Ultra Simplifies Histone Preparation for LC-MS/MS
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00141451" target="_blank" >RIV/00216224:14740/25:00141451 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c02238" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.analchem.5c02238</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.analchem.5c02238" target="_blank" >10.1021/acs.analchem.5c02238</a>
Alternative languages
Result language
angličtina
Original language name
Arg-C Ultra Simplifies Histone Preparation for LC-MS/MS
Original language description
Arginine-specific cleavage is the primary method used to prepare lysine-rich histone proteins in bottom-up proteomics. As the Arg-C enzyme has demonstrated suboptimal specificity, cleavage at the carboxyl side of arginine residues is typically achieved through the chemical derivatization of lysines followed by trypsin digestion. Recent improvements in proteolytic enzymes are reflected in the introduction of Arg-C Ultra, a recombinant proteinase with a substantially improved digestion specificity. Here, using mammalian histone extract, we demonstrate that Arg-C Ultra facilitates histone preparation for LC-MS/MS. We show the performance of Arg-C Ultra in terms of digestion specificity, number of modified forms identified, and yield of quantitative information compared with Arg-C and trypsin digestion combined with chemical derivatization with trimethylacetic anhydride. Importantly, we show that chemical derivatization at the peptide level, i.e., after Arg-C Ultra digestion, is still necessary to improve the quantification of short histone peptidoforms as well as positional isomers.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Analytical chemistry
ISSN
0003-2700
e-ISSN
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Volume of the periodical
97
Issue of the periodical within the volume
24
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
12486-12492
UT code for WoS article
001508703400001
EID of the result in the Scopus database
2-s2.0-105008485358