<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>101</volume><submitter>Rajput P</submitter><funding>National Institute of Food and Agriculture</funding><pubmed_abstract>Milk proteins serve as nutrition and affect neonate development and immunity through their bioactivity. Post-translational modifications of proteins affect their bioactivity. Glycosylation is the attachment of sugar moieties to proteins, with attachment of glycans to asparagine indicated as N-linked glycosylation. Our objective was to characterize N-linked glycosylated proteins in homogenate swine milk samples collected from sows (n = 5/6) during farrowing to represent colostrum and on days 3 and 14 post-farrowing to represent transitional and mature milk, respectively. Glycopeptides were isolated with lectin-based extraction and treated with Peptide N-glycosidase F (PNGase F) to identify N-linked glycosylation sites. Purified glycopeptides were analyzed by label-free liquid chromatography</pubmed_abstract><journal>Journal of animal science</journal><pagination>skac426</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9940737</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Characterization of sow milk N-linked glycoproteome over the course of lactation.</pubmed_title><pmcid>PMC9940737</pmcid><pubmed_authors>Minor RC</pubmed_authors><pubmed_authors>Aryal UK</pubmed_authors><pubmed_authors>Bhide K</pubmed_authors><pubmed_authors>Krishnamurthy S</pubmed_authors><pubmed_authors>Rajput P</pubmed_authors><pubmed_authors>Casey TM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Characterization of sow milk N-linked glycoproteome over the course of lactation.</name><description>Milk proteins serve as nutrition and affect neonate development and immunity through their bioactivity. Post-translational modifications of proteins affect their bioactivity. Glycosylation is the attachment of sugar moieties to proteins, with attachment of glycans to asparagine indicated as N-linked glycosylation. Our objective was to characterize N-linked glycosylated proteins in homogenate swine milk samples collected from sows (n = 5/6) during farrowing to represent colostrum and on days 3 and 14 post-farrowing to represent transitional and mature milk, respectively. Glycopeptides were isolated with lectin-based extraction and treated with Peptide N-glycosidase F (PNGase F) to identify N-linked glycosylation sites. Purified glycopeptides were analyzed by label-free liquid chromatography</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jan</publication><modification>2026-05-18T03:15:27.822Z</modification><creation>2025-04-04T19:01:33.66Z</creation></dates><accession>S-EPMC9940737</accession><cross_references><pubmed>36585837</pubmed><doi>10.1093/jas/skac426</doi></cross_references></HashMap>