Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/36350
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Wu, JY | - |
dc.creator | Chen, X | - |
dc.creator | Siu, KC | - |
dc.date.accessioned | 2016-04-20T09:37:49Z | - |
dc.date.available | 2016-04-20T09:37:49Z | - |
dc.identifier.issn | 1661-6596 | - |
dc.identifier.uri | http://hdl.handle.net/10397/36350 | - |
dc.language.iso | en | en_US |
dc.publisher | Molecular 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.rights | The 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/ijms151017318 | en_US |
dc.subject | Cordyceps sinensis | en_US |
dc.subject | Glycopeptide | en_US |
dc.subject | Structure | en_US |
dc.subject | Antioxidant | en_US |
dc.subject | Cell protection | en_US |
dc.title | Isolation and structure characterization of an antioxidative glycopeptide from mycelial culture broth of a medicinal fungus | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.spage | 17318 | - |
dc.identifier.epage | 17332 | - |
dc.identifier.volume | 15 | - |
dc.identifier.issue | 10 | - |
dc.identifier.doi | 10.3390/ijms151017318 | - |
dcterms.abstract | A 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.accessRights | open access | en_US |
dcterms.bibliographicCitation | International journal of molecular sciences, Oct. 2014, v. 15, no. 10, p. 17318-17332 | - |
dcterms.isPartOf | International journal of molecular sciences | - |
dcterms.issued | 2014 | - |
dc.identifier.isi | WOS:000344457200008 | - |
dc.identifier.scopus | 2-s2.0-84907834050 | - |
dc.identifier.pmid | 25268609 | - |
dc.identifier.eissn | 1422-0067 | - |
dc.identifier.rosgroupid | 2014002194 | - |
dc.description.ros | 2014-2015 > Academic research: refereed > Publication in refereed journal | - |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
Files in This Item:
File | Description | Size | Format | |
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Wu_Structure_Antioxidative_Glycopeptide.pdf | 1.09 MB | Adobe PDF | View/Open |
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