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A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces
A novel 68 kDa laccase was purified from the mycorrhizal fungus Agaricus placomyces by 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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471028/ https://www.ncbi.nlm.nih.gov/pubmed/23093860 http://dx.doi.org/10.1155/2012/736472 |
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author | Sun, Jian Chen, Qing-Jun Cao, Qing-Qin Wu, Ying-Ying Xu, Li-Jing Zhu, Meng-Juan Ng, Tzi-Bun Wang, He-Xiang Zhang, Guo-Qing |
author_facet | Sun, Jian Chen, Qing-Jun Cao, Qing-Qin Wu, Ying-Ying Xu, Li-Jing Zhu, Meng-Juan Ng, Tzi-Bun Wang, He-Xiang Zhang, Guo-Qing |
author_sort | Sun, Jian |
collection | PubMed |
description | A novel 68 kDa laccase was purified from the mycorrhizal fungus Agaricus placomyces by 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 for A. placomyces laccase 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, K(m) values 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 IC(50) of 1.8 μM, 1.7 μM, and 1.25 μM, respectively, signifying that it is an antipathogenic protein. |
format | Online Article Text |
id | pubmed-3471028 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-34710282012-10-23 A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces Sun, Jian Chen, Qing-Jun Cao, Qing-Qin Wu, Ying-Ying Xu, Li-Jing Zhu, Meng-Juan Ng, Tzi-Bun Wang, He-Xiang Zhang, Guo-Qing J Biomed Biotechnol Research Article A novel 68 kDa laccase was purified from the mycorrhizal fungus Agaricus placomyces by 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 for A. placomyces laccase 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, K(m) values 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 IC(50) of 1.8 μM, 1.7 μM, and 1.25 μM, respectively, signifying that it is an antipathogenic protein. Hindawi Publishing Corporation 2012 2012-10-03 /pmc/articles/PMC3471028/ /pubmed/23093860 http://dx.doi.org/10.1155/2012/736472 Text en Copyright © 2012 Jian Sun et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Sun, Jian Chen, Qing-Jun Cao, Qing-Qin Wu, Ying-Ying Xu, Li-Jing Zhu, Meng-Juan Ng, Tzi-Bun Wang, He-Xiang Zhang, Guo-Qing A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title | A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title_full | A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title_fullStr | A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title_full_unstemmed | A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title_short | A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal Fungus Agaricus placomyces |
title_sort | laccase with antiproliferative and hiv-i reverse transcriptase inhibitory activities from the mycorrhizal fungus agaricus placomyces |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471028/ https://www.ncbi.nlm.nih.gov/pubmed/23093860 http://dx.doi.org/10.1155/2012/736472 |
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