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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- Dr Sze, Cho Wing

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Publisher Website: 10.2174/092986610791498966
Scopus: eid_2-s2.0-77958065455
PMID: 19807674
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Title	Purification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)
Authors	Wong, JH3 Ng, TB3 Jiang, Y2 Liu, F2 Sze, SCW1 Zhang, KY1
Keywords	Isolation Laccase Mushroom Pleurotus cornucopiae
Issue Date	2010
Publisher	Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
Citation	Protein And Peptide Letters, 2010, v. 17 n. 8, p. 1040-1047 [How to Cite?] DOI: http://dx.doi.org/10.2174/092986610791498966
Abstract	A 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.
ISSN	0929-8665 2011 Impact Factor: 1.942 2011 SCImago Journal Rankings: 0.145
DOI	http://dx.doi.org/10.2174/092986610791498966
ISI Accession Number ID	WOS:000281419200012
References	References in Scopus

DC Field	Value
dc.contributor.author	Wong, JH
dc.contributor.author	Ng, TB
dc.contributor.author	Jiang, Y
dc.contributor.author	Liu, F
dc.contributor.author	Sze, SCW
dc.contributor.author	Zhang, KY
dc.date.accessioned	2011-09-23T06:24:07Z
dc.date.available	2011-09-23T06:24:07Z
dc.date.issued	2010
dc.description.abstract	A 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.nature	Link_to_subscribed_fulltext
dc.identifier.citation	Protein And Peptide Letters, 2010, v. 17 n. 8, p. 1040-1047 [How to Cite?] DOI: http://dx.doi.org/10.2174/092986610791498966
dc.identifier.citeulike	7403835
dc.identifier.doi	http://dx.doi.org/10.2174/092986610791498966
dc.identifier.epage	1047
dc.identifier.hkuros	192433
dc.identifier.hkuros	171307
dc.identifier.isi	WOS:000281419200012
dc.identifier.issn	0929-8665 2011 Impact Factor: 1.942 2011 SCImago Journal Rankings: 0.145
dc.identifier.issue	8
dc.identifier.openurl
dc.identifier.pmid	19807674
dc.identifier.scopus	eid_2-s2.0-77958065455
dc.identifier.spage	1040
dc.identifier.uri	http://hdl.handle.net/10722/141038
dc.identifier.volume	17
dc.language	eng
dc.publisher	Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
dc.publisher.place	Netherlands
dc.relation.ispartof	Protein and Peptide Letters
dc.relation.references	References in Scopus
dc.subject.mesh	HIV Reverse Transcriptase - antagonists and inhibitors
dc.subject.mesh	HIV-1 - drug effects - enzymology
dc.subject.mesh	Laccase - chemistry - isolation and purification - metabolism - pharmacology
dc.subject.mesh	Pleurotus - enzymology
dc.subject.mesh	Reverse Transcriptase Inhibitors - isolation and purification - metabolism - pharmacology
dc.subject	Isolation
dc.subject	Laccase
dc.subject	Mushroom
dc.subject	Pleurotus cornucopiae
dc.title	Purification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)
dc.type	Article

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Author Affiliations

The University of Hong Kong Li Ka Shing Faculty of Medicine
Nankai University
Chinese University of Hong Kong

Article: Purification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (pleurotus cornucopiae)

The HKU Scholars Hub has contact details for these author(s).