Data di Pubblicazione:
2014
Abstract:
A simple procedure is proposed for selective protein
solubilization and trypsin digestion, followed by off-line liquid chromatography-
matrix assisted laser desorption ionization mass spectrometry (LC-
MALDI MS) analysis of Oenococcus oeni (O. oeni) bacterium. Peptides were
identified from tryptic digests using sequencing by tandem mass
spectrometry and database searches. Cytoplasmic and membrane related
proteins (MRP) were identified in the O. oeni bacterium. MS/MS data
analysis points out 13 peptides having one point mutation from 9 proteins.
The major microheterogeneity was found for Zn-dependent alcohol
dehydrogenase (Zn-ADH, Q04GE6) and 60 kDa chaperonin (GroEL,
Q04E64) that are involved in methionine catabolism and post-translational
protein folding, respectively. MS/MS data processing also leads to the
identification of 34 unique phosphorylation sites from 19 phosphoproteins.
solubilization and trypsin digestion, followed by off-line liquid chromatography-
matrix assisted laser desorption ionization mass spectrometry (LC-
MALDI MS) analysis of Oenococcus oeni (O. oeni) bacterium. Peptides were
identified from tryptic digests using sequencing by tandem mass
spectrometry and database searches. Cytoplasmic and membrane related
proteins (MRP) were identified in the O. oeni bacterium. MS/MS data
analysis points out 13 peptides having one point mutation from 9 proteins.
The major microheterogeneity was found for Zn-dependent alcohol
dehydrogenase (Zn-ADH, Q04GE6) and 60 kDa chaperonin (GroEL,
Q04E64) that are involved in methionine catabolism and post-translational
protein folding, respectively. MS/MS data processing also leads to the
identification of 34 unique phosphorylation sites from 19 phosphoproteins.
Tipologia CRIS:
01.01 Articolo in rivista
Keywords:
Oenoccoccus oeni; MALDI; mass spectrometry; enzymes; phosphorylation; point mutation; shotgun approach; bacteria
Elenco autori:
Cappello, MARIA STELLA
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