Abstract |
A laccase, with HIV-1 reverse transcriptase inhibitory activity (IC(50)=12.7 μM) and antiproliferative activity against HepG2 cells (IC(50)=5.6 μM) and MCF7 cells (IC(50)=6.5 μM), was purified from fresh fruiting bodies of the edible white common Agrocybe cylindracea mushroom. The laccase, which had a novel N-terminal sequence, displayed a molecular mass of 58 kDa within the range reported for most other mushroom laccases. The purification protocol entailed ion exchange chromatography on DEAE-cellulose, SP- Sepharose, and Q- Sepharose and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q- Sepharose, but unadsorbed on SP- Sepharose. Its optimum pH was pH 3-4 and its optimum temperature was 50°C. The activity of the isolated laccase differed from one substrate to another. The ranking was ABTS>N,N-dimethyl-1,4-phenylenediamine> hydroquinone> catechol>2-methylcatechol> pyrogallol.
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Authors | D D Hu, R Y Zhang, G Q Zhang, H X Wang, T B Ng |
Journal | Phytomedicine : international journal of phytotherapy and phytopharmacology
(Phytomedicine)
Vol. 18
Issue 5
Pg. 374-9
(Mar 15 2011)
ISSN: 1618-095X [Electronic] Germany |
PMID | 20739163
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2010 Elsevier GmbH. All rights reserved. |
Chemical References |
- Laccase
- HIV Reverse Transcriptase
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Topics |
- Agrocybe
(enzymology)
- Amino Acid Sequence
- Cell Line, Tumor
- Cell Proliferation
(drug effects)
- Chromatography, Gel
- Chromatography, Ion Exchange
- Electrophoresis, Polyacrylamide Gel
- Fruiting Bodies, Fungal
(enzymology)
- HIV Reverse Transcriptase
(antagonists & inhibitors)
- Humans
- Hydrogen-Ion Concentration
- Laccase
(chemistry, isolation & purification, metabolism, pharmacology)
- Molecular Weight
- Sequence Homology, Amino Acid
- Substrate Specificity
- Temperature
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