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In-gel protein digestion using acidic methanol produces a highly selective methylation of glutamic acid residues.
- Source :
-
Journal of proteomics [J Proteomics] 2024 Jul 30; Vol. 304, pp. 105229. Date of Electronic Publication: 2024 Jun 14. - Publication Year :
- 2024
-
Abstract
- Mass-tolerant open search methods allow the high-throughput analysis of modified peptides by mass spectrometry. These techniques have paved the way to unbiased analysis of post-translational modifications in biological contexts, as well as of chemical modifications produced during the manipulation of protein samples. In this work, we have analyzed in-depth a wide variety of samples of different biological origin, including cells, extracellular vesicles, secretomes, centrosomes and tissue preparations, using Comet-ReCom, a recently improved version of the open search engine Comet-PTM. Our results demonstrate that glutamic acid residues undergo intensive methyl esterification when protein digestion is performed using in-gel techniques, but not using gel-free approaches. This effect was highly specific to Glu and was not found for other methylable residues such as Asp.<br />Competing Interests: Declaration of competing interest The authors declare no competing interests.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)
Details
- Language :
- English
- ISSN :
- 1876-7737
- Volume :
- 304
- Database :
- MEDLINE
- Journal :
- Journal of proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 38880355
- Full Text :
- https://doi.org/10.1016/j.jprot.2024.105229