In-depth glycoproteomic characterization of γ-conglutin by high-resolution accurate mass spectrometry.

ABSTRACT: The molecular characterization of bioactive food components is necessary for understanding the mechanisms of their beneficial or detrimental effects on human health. This study focused on γ-conglutin, a well-known lupin seed N-glycoprotein with health-promoting properties and controversial allergenic potential. Given the importance of N-glycosylation for the functional and structural characteristics of proteins, we studied the purified protein by a mass spectrometry-based glycoproteomic approach able to identify the structure, micro-heterogeneity and attachment site of the bound N-glycan(s), and to provide extensive coverage of the protein sequence. The peptide/N-glycopeptide mixtures generated by enzymatic digestion (with or without N-deglycosylation) were analyzed by high-resolution accu

SUBMITTER: Schiarea S 

PROVIDER: S-EPMC3771881 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature