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
Rok vydání: 2012
Předmět:
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