{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T22:47:15Z","timestamp":1768517235836,"version":"3.49.0"},"reference-count":39,"publisher":"Wiley","issue":"15","license":[{"start":{"date-parts":[[2012,6,15]],"date-time":"2012-06-15T00:00:00Z","timestamp":1339718400000},"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":[[2012,8]]},"abstract":"<jats:p>Most of the phospholipases A<jats:sub>2<\/jats:sub> (PLA<jats:sub>2<\/jats:sub>; <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.chem.qmul.ac.uk\/iubmb\/enzyme\/EC3\/1\/1\/4.html\">EC3.1.1.4<\/jats:ext-link>) variants isolated so far from snake venoms are nonglycosylated enzymes. In the present study, we purified an active glycosylated PLA<jats:sub>2<\/jats:sub> and an inactive nonglycosylated Lys49\u2010like PLA<jats:sub>2<\/jats:sub> from two geographical venom samples of <jats:italic>Tropidolaemus<\/jats:italic>. The PLA<jats:sub>2<\/jats:sub> variants from the two samples have rather different N\u2010terminal sequences, implying that the samples were probably derived from two species (<jats:italic>Tropidolaemus\u2003subannulatus<\/jats:italic> and <jats:italic>Tropidolaemus\u2003wagleri<\/jats:italic>). The active PLA<jats:sub>2<\/jats:sub>s from Sulawesi and Sumatra venoms were designated as Tsu\u2010E6 and Twa\u2010E6, respectively, as a result of the presence of their conserved Glu6 residue. Tsu\u2010E6 inhibited ADP\u2010induced aggregation of mouse and human platelets. Twa\u2010E6 stimulated the aggregation of mouse platelets but inhibited the aggregation of human platelets. Both PLA<jats:sub>2<\/jats:sub>s were found to be glycosylated at Asn14. Using MALDI\u2010TOF analysis, the released glycans were shown to comprise complex type oligosaccharides without sialylation. This is the first glycan structure of the snake venom PLA<jats:sub>2<\/jats:sub> to be solved. Furthermore, the enzymatic removal of glycans from both PLA<jats:sub>2<\/jats:sub>s did not significantly alter their effects on lipid hydrolysis and platelet aggregation. The thermostability of glycosylated Twa\u2010E6 was also found to be as good as that of other homologous PLA<jats:sub>2<\/jats:sub>s. The presence of these oligosaccharides in PLA<jats:sub>2<\/jats:sub>s warrants further analyses, which may provide useful insights into the functional regulation of these biomolecules.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2012.08648.x","type":"journal-article","created":{"date-parts":[[2012,5,26]],"date-time":"2012-05-26T15:25:34Z","timestamp":1338045934000},"page":"2672-2682","source":"Crossref","is-referenced-by-count":18,"title":["Glycan structures and intrageneric variations of venom acidic phospholipases A<sub>2<\/sub> from <i>Tropidolaemus<\/i> 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