{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Santamaria L"],"funding":["Agriculture and Agri-Food Canada"],"pagination":["14844-14850"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11228969"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["72(26)"],"pubmed_abstract":["The 11S globulin legumin typically accounts for approximately 3% of the total protein in common beans (<i>Phaseolus vulgaris</i>). It was previously reported that a legumin peptide of approximately 20 kDa is resistant to pepsin digestion. Sequence prediction suggested that the pepsin-resistant peptide is located at the C-terminal end of the α-subunit, within a glutamic acid-rich domain, overlapping with a chymotrypsin-resistant peptide. Using purified legumin, the peptide of approximately 20 kDa was found to be resistant to pepsin digestion in a pH-dependent manner, and its location was determined by two-dimensional gel electrophoresis and LC-MS-MS. The location of the chymotrypsin-resistant peptide was confirmed by immunoblotting with peptide-specific polyclonal antibodies. The presence o"],"journal":["Journal of agricultural and food chemistry"],"pubmed_title":["Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean (<i>Phaseolus vulgaris</i> L.)."],"pmcid":["PMC11228969"],"funding_grant_id":["J-000562"],"pubmed_authors":["Pajak A","House JD","Marsolais F","Santamaria L"],"additional_accession":[]},"is_claimable":false,"name":"Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean (<i>Phaseolus vulgaris</i> L.).","description":"The 11S globulin legumin typically accounts for approximately 3% of the total protein in common beans (<i>Phaseolus vulgaris</i>). It was previously reported that a legumin peptide of approximately 20 kDa is resistant to pepsin digestion. Sequence prediction suggested that the pepsin-resistant peptide is located at the C-terminal end of the α-subunit, within a glutamic acid-rich domain, overlapping with a chymotrypsin-resistant peptide. Using purified legumin, the peptide of approximately 20 kDa was found to be resistant to pepsin digestion in a pH-dependent manner, and its location was determined by two-dimensional gel electrophoresis and LC-MS-MS. The location of the chymotrypsin-resistant peptide was confirmed by immunoblotting with peptide-specific polyclonal antibodies. The presence o","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T07:37:43.867Z","creation":"2025-04-04T11:24:38.376Z"},"accession":"S-EPMC11228969","cross_references":{"pubmed":["38885440"],"doi":["10.1021/acs.jafc.3c08744"]}}