{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T07:10:28Z","timestamp":1781939428442,"version":"3.54.5"},"reference-count":41,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2011,9,8]],"date-time":"2011-09-08T00:00:00Z","timestamp":1315440000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2011,10]]},"abstract":"<jats:p>Milk provides nutritional, immunological and developmental components for newborns. Whereas identification of such components has been performed by targeting proteins and free oligosaccharides, structural and functional analyses of the N\u2010glycome of milk glycoproteins are scarce. In this study, we investigated, for the first time, the alterations of the bovine milk N\u2010glycome during early lactation (1\u2003day, 1, 2, 3 and 4\u2003weeks postpartum), characterizing more than 80\u2003N\u2010glycans. The glycomic profile of colostrum on day\u20031 after calving differed substantially from that in other periods during early lactation. The proteins in colostrum obtained 1\u2003day postpartum were more highly sialylated than milk samples obtained at other time points, and the N\u2010glycolylneuraminic acid (Neu5Gc)\/N\u2010acetylneuraminic acid (Neu5Ac) ratio was significantly higher on day\u20031, showing a gradual decline with time. In order to dissect the N\u2010glycome of colostrum, alterations of the N\u2010glycosylation profile of major bovine milk proteins during the early lactation stage were elucidated, revealing that the alteration is largely attributable to qualitative and quantitative N\u2010glycosylation changes of IgG, the major glycoprotein in colostrum. Furthermore, by preparing and analyzing IgGs in which the N\u2010glycan structure and subtypes were well characterized, we found that the interaction between IgG and FcRn was not affected by the structure of the N\u2010glycans attached to IgG. We also found that bovine FcRn binds IgG<jats:sub>2<\/jats:sub> better than IgG<jats:sub>1<\/jats:sub>, strongly suggesting that the role of FcRn in the bovine mammary gland is to recycle IgG<jats:sub>2<\/jats:sub> from the udder to blood, rather than to secrete IgG<jats:sub>1<\/jats:sub> into colostrum.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2011.08299.x","type":"journal-article","created":{"date-parts":[[2011,8,12]],"date-time":"2011-08-12T01:06:28Z","timestamp":1313111188000},"page":"3769-3781","source":"Crossref","is-referenced-by-count":64,"title":["Alteration of the N\u2010glycome of bovine milk glycoproteins during early 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