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Article: Purification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)
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TitlePurification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)
 
AuthorsWong, JH3
Ng, TB3
Jiang, Y2
Liu, F2
Sze, SCW1
Zhang, KY1
 
KeywordsIsolation
Laccase
Mushroom
Pleurotus cornucopiae
 
Issue Date2010
 
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
 
CitationProtein And Peptide Letters, 2010, v. 17 n. 8, p. 1040-1047 [How to Cite?]
DOI: http://dx.doi.org/10.2174/092986610791498966
 
AbstractA 66-kDa laccase, with an N-terminal sequence different from those of other mushroom laccases, was purified from fresh fruiting bodies of the edible mushroom Pleurotus cornucopiae by using affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono Q and gel filtration on Superdex 75. The procedure resulted in a 16-fold purification and a specific enzyme activity of 17.3 U mg -1. The optimum pH and temperature for the purified laccase were pH 4 and 40°C, respectively. This laccase inhibited proliferation of murine leukemia cell line L1210 and human hepatoma cell line HepG2, and reduced the activity of HIV-1 reverse transcriptase with an IC 50 of 22 μM. There was neither mitogenic activity toward mouse splenocytes, nor hemagglutinating/hemolytic activity toward rabbit erythrocytes. This study yielded information about the potentially exploitable activities of P. cornucopiae laccase. © 2010 Bentham Science Publishers Ltd.
 
ISSN0929-8665
2013 Impact Factor: 1.735
2013 SCImago Journal Rankings: 0.571
 
DOIhttp://dx.doi.org/10.2174/092986610791498966
 
ISI Accession Number IDWOS:000281419200012
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorWong, JH
 
dc.contributor.authorNg, TB
 
dc.contributor.authorJiang, Y
 
dc.contributor.authorLiu, F
 
dc.contributor.authorSze, SCW
 
dc.contributor.authorZhang, KY
 
dc.date.accessioned2011-09-23T06:24:07Z
 
dc.date.available2011-09-23T06:24:07Z
 
dc.date.issued2010
 
dc.description.abstractA 66-kDa laccase, with an N-terminal sequence different from those of other mushroom laccases, was purified from fresh fruiting bodies of the edible mushroom Pleurotus cornucopiae by using affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono Q and gel filtration on Superdex 75. The procedure resulted in a 16-fold purification and a specific enzyme activity of 17.3 U mg -1. The optimum pH and temperature for the purified laccase were pH 4 and 40°C, respectively. This laccase inhibited proliferation of murine leukemia cell line L1210 and human hepatoma cell line HepG2, and reduced the activity of HIV-1 reverse transcriptase with an IC 50 of 22 μM. There was neither mitogenic activity toward mouse splenocytes, nor hemagglutinating/hemolytic activity toward rabbit erythrocytes. This study yielded information about the potentially exploitable activities of P. cornucopiae laccase. © 2010 Bentham Science Publishers Ltd.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationProtein And Peptide Letters, 2010, v. 17 n. 8, p. 1040-1047 [How to Cite?]
DOI: http://dx.doi.org/10.2174/092986610791498966
 
dc.identifier.citeulike7403835
 
dc.identifier.doihttp://dx.doi.org/10.2174/092986610791498966
 
dc.identifier.epage1047
 
dc.identifier.hkuros192433
 
dc.identifier.hkuros171307
 
dc.identifier.isiWOS:000281419200012
 
dc.identifier.issn0929-8665
2013 Impact Factor: 1.735
2013 SCImago Journal Rankings: 0.571
 
dc.identifier.issue8
 
dc.identifier.openurl
 
dc.identifier.pmid19807674
 
dc.identifier.scopuseid_2-s2.0-77958065455
 
dc.identifier.spage1040
 
dc.identifier.urihttp://hdl.handle.net/10722/141038
 
dc.identifier.volume17
 
dc.languageeng
 
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
 
dc.publisher.placeNetherlands
 
dc.relation.ispartofProtein and Peptide Letters
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshHIV Reverse Transcriptase - antagonists and inhibitors
 
dc.subject.meshHIV-1 - drug effects - enzymology
 
dc.subject.meshLaccase - chemistry - isolation and purification - metabolism - pharmacology
 
dc.subject.meshPleurotus - enzymology
 
dc.subject.meshReverse Transcriptase Inhibitors - isolation and purification - metabolism - pharmacology
 
dc.subjectIsolation
 
dc.subjectLaccase
 
dc.subjectMushroom
 
dc.subjectPleurotus cornucopiae
 
dc.titlePurification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Nankai University
  3. Chinese University of Hong Kong