A laccase with antiproliferative and HIV-I reverse transcriptase inhibitory activities from the mycorrhizal fungus Agaricus placomyces
Autor: | Mengjuan Zhu, Qing-Qin Cao, Ying-Ying Wu, Jian Sun, H. X. Wang, Li-Jing Xu, Guoqing Zhang, Qing-Jun Chen, Tzi Bun Ng |
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Rok vydání: | 2012 |
Předmět: |
Article Subject
lcsh:Biotechnology Health Toxicology and Mutagenesis Agaricus Ion chromatography lcsh:Medicine Biology Fungal Proteins chemistry.chemical_compound lcsh:TP248.13-248.65 Genetics Humans Molecular Biology Cell Proliferation chemistry.chemical_classification Laccase Fungal protein ABTS Hydroquinone lcsh:R General Medicine Hep G2 Cells Neoplasms Experimental biology.organism_classification HIV Reverse Transcriptase Hep G2 Enzyme chemistry Biochemistry MCF-7 Cells Molecular Medicine Reverse Transcriptase Inhibitors Biotechnology Research Article |
Zdroj: | Journal of Biomedicine and Biotechnology Journal of Biomedicine and Biotechnology, Vol 2012 (2012) |
ISSN: | 1110-7251 |
Popis: | A novel 68 kDa laccase was purified from the mycorrhizal fungusAgaricus placomycesby utilizing a procedure that comprised three successive steps of ion exchange chromatography and gel filtration as the final step. The monomeric enzyme exhibited the N-terminal amino acid sequence of DVIGPQAQVTLANQD, which showed only a low extent of homology to sequences of other fungal laccases. The optimal temperature forA. placomyceslaccase was 30°C, and optimal pH values for laccase activity towards the substrates 2,7′-azinobis[3-ethylbenzothiazolone-6-sulfonic acid] diammonium salt (ABTS) and hydroquinone were 5.2 and 6.8, respectively. The laccase displayed, at 30°C and pH 5.2,Kmvalues of 0.392 mM towards hydroquinone and 0.775 mM towards ABTS. It potently suppressed proliferation of MCF 7 human breast cancer cells and Hep G2 hepatoma cells and inhibited human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) activity with an IC50of 1.8 μM, 1.7 μM, and 1.25 μM, respectively, signifying that it is an antipathogenic protein. |
Databáze: | OpenAIRE |
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