<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Santamaria L</submitter><funding>Agriculture and Agri-Food Canada</funding><pagination>14844-14850</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11228969</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>72(26)</volume><pubmed_abstract>The 11S globulin legumin typically accounts for approximately 3% of the total protein in common beans (&lt;i>Phaseolus vulgaris&lt;/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</pubmed_abstract><journal>Journal of agricultural and food chemistry</journal><pubmed_title>Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean (&lt;i>Phaseolus vulgaris&lt;/i> L.).</pubmed_title><pmcid>PMC11228969</pmcid><funding_grant_id>J-000562</funding_grant_id><pubmed_authors>Pajak A</pubmed_authors><pubmed_authors>House JD</pubmed_authors><pubmed_authors>Marsolais F</pubmed_authors><pubmed_authors>Santamaria L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean (&lt;i>Phaseolus vulgaris&lt;/i> L.).</name><description>The 11S globulin legumin typically accounts for approximately 3% of the total protein in common beans (&lt;i>Phaseolus vulgaris&lt;/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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jul</publication><modification>2026-06-01T07:37:43.867Z</modification><creation>2025-04-04T11:24:38.376Z</creation></dates><accession>S-EPMC11228969</accession><cross_references><pubmed>38885440</pubmed><doi>10.1021/acs.jafc.3c08744</doi></cross_references></HashMap>