In-gel protein digestion using acidic methanol produces a highly selective methylation of glutamic acid residues.
J Proteomics
; 304: 105229, 2024 Jul 30.
Article
em En
| MEDLINE
| ID: mdl-38880355
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ácido Glutâmico
/
Metanol
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article