Abstract:
:A method for quantitative proteomic analysis based on the selective isolation of multiply charged peptides (RH peptides) containing arginine and histidine residues is described. Two pools of proteins are digested in tandem with lysyl-endopeptidase and trypsin and the primary amino groups of proteolytic peptides are separately labeled with d3- and d0-acetic anhydride. This reaction has a dual purpose: (i) to allow the relative protein quantification in two different conditions and (ii) to restrict the positive charges of peptides to the presence of arginine and histidine. The N-acylated peptides are separated by cation-exchange chromatography into two groups, neutral and singly charged peptides (R+H
journal_name
Proteomicsjournal_title
Proteomicsauthors
Sánchez A,González LJ,Betancourt L,Gil J,Besada V,Fernández-de-Cossío J,Rodríguez-Ulloa A,Marrero K,Alvarez F,Fando R,Padrón Gdoi
10.1002/pmic.200500836subject
Has Abstractpub_date
2006-08-01 00:00:00pages
4444-55issue
16eissn
1615-9853issn
1615-9861journal_volume
6pub_type
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