Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/36350
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dc.contributorDepartment of Applied Biology and Chemical Technology-
dc.creatorWu, JY-
dc.creatorChen, X-
dc.creatorSiu, KC-
dc.date.accessioned2016-04-20T09:37:49Z-
dc.date.available2016-04-20T09:37:49Z-
dc.identifier.issn1661-6596-
dc.identifier.urihttp://hdl.handle.net/10397/36350-
dc.language.isoenen_US
dc.publisherMolecular Diversity Preservation International (MDPI)en_US
dc.rights© 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).en_US
dc.rightsThe following publication Wu, J. Y., Chen, X., & Siu, K. C. (2014). Isolation and structure characterization of an antioxidative glycopeptide from mycelial culture broth of a medicinal fungus. International Journal of Molecular Sciences, 15(10), (Suppl. ), 17318-17332 is available athttps://dx.doi.org/10.3390/ijms151017318en_US
dc.subjectCordyceps sinensisen_US
dc.subjectGlycopeptideen_US
dc.subjectStructureen_US
dc.subjectAntioxidanten_US
dc.subjectCell protectionen_US
dc.titleIsolation and structure characterization of an antioxidative glycopeptide from mycelial culture broth of a medicinal fungusen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.spage17318-
dc.identifier.epage17332-
dc.identifier.volume15-
dc.identifier.issue10-
dc.identifier.doi10.3390/ijms151017318-
dcterms.abstractA novel glycopeptide (Cs-GP1) with an average molecular weight (Mw) of 6.0 kDa was isolated and purified by column chromatography from the lower Mw fraction of exopolysaccharide (EPS) produced by a medicinal fungus Cordyceps sinensis Cs-HK1. Its carbohydrate moiety was mainly composed of glucose and mannose at 3.2:1.0 mole ratio, indicating an O-linked glycopeptide. The peptide chain contained relatively high mole ratios of aspartic acid, glutamic acid and glycine (3.3-3.5 relative to arginine) but relatively low ratios of tyrosine and histidine. The peptide chain sequence analyzed after trypsin digestion by LC-MS was KNGIFQFGEDCAAGSISHELGGFREFREFLKQAGLE. Cs-GP1 exhibited remarkable antioxidant capacity with a Trolox equivalent antioxidant capacity of 1183.8 mu mol/g and a ferric reducing ability of 611.1 mu mol Fe(II)/g, and significant protective effect against H2O2-induced PC12 cell injury at a minimum dose of 10 mu g/mL. This is the first report on the structure and bioactivity of an extracellular glycopeptide from the Cordyceps species.-
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationInternational journal of molecular sciences, Oct. 2014, v. 15, no. 10, p. 17318-17332-
dcterms.isPartOfInternational journal of molecular sciences-
dcterms.issued2014-
dc.identifier.isiWOS:000344457200008-
dc.identifier.scopus2-s2.0-84907834050-
dc.identifier.pmid25268609-
dc.identifier.eissn1422-0067-
dc.identifier.rosgroupid2014002194-
dc.description.ros2014-2015 > Academic research: refereed > Publication in refereed journal-
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumberOA_IR/PIRAen_US
dc.description.pubStatusPublisheden_US
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