https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:46784 Wed 30 Nov 2022 13:21:59 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:37132 Wed 19 Aug 2020 14:02:44 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:30252 N-linked sialylated glycoproteins in rat epididymal sperm and investigate whether they are regulated during epididymal transit. Sialylated glycopeptides from caput, corpus, and cauda spermatozoa were enriched using titanium dioxide beads. Bound N-linked glycopeptides were released by enzymatic deglycosylation using PNGase F and then analyzed by liquid chromatography tandem-mass spectrometry. A total of 92 unique N-linked sialylated glycopeptides were identified from 65 different proteins. These included members of the disintegrin and metalloproteinase domain-containing protein family (ADAM), Basigin, and Testis-expressed protein 101 (TEX101). Remarkably, label-free quantification showed that more than half of these peptides (48/92) were regulated during epididymal transit. Of interest, the protein TEX101 exhibited PNGase F-resistant deglycosylation under the conditions used in this study. The results from this study showed that changes in the N-linked sialoglycoprotein profile is a major hallmark of sperm maturation in rats.]]> Wed 11 Apr 2018 17:21:10 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:42360 Mon 22 Aug 2022 14:01:23 AEST ]]>