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J Biomed Biotechnol ; 2012: 736472, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23093860

RESUMO

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.


Assuntos
Agaricus/enzimologia , Transcriptase Reversa do HIV/antagonistas & inibidores , Lacase/administração & dosagem , Lacase/metabolismo , Neoplasias Experimentais/tratamento farmacológico , Inibidores da Transcriptase Reversa/química , Proliferação de Células/efeitos dos fármacos , Proteínas Fúngicas/metabolismo , Proteínas Fúngicas/farmacologia , Células Hep G2 , Humanos , Células MCF-7 , Neoplasias Experimentais/patologia
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