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Biotechnol Appl Biochem ; 60(4): 393-8, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-24033593


A 36-kDa protein, with an N-terminal sequence highly homologous to polygalacturonase (PG) inhibiting proteins, was isolated from small brown-eyed cowpea seeds. The protein was unadsorbed on diethylaminoethyl cellulose but adsorbed on both Affi-gel blue gel and SP-sepharose. It inhibited mycelial growth in the fungus Mycosphaerella arachidicola with an half-maximal (50%) inhibitory concentration (IC50 ) of 3.3 µM. It reduced [methyl-(3) H] thymidine incorporation into MBL2 lymphoma and L1210 leukemia cells with an IC50 of 7.4 and 5.4 µM, respectively. It inhibited human immunodeficiency virus type 1 (HIV-1) reverse transcriptase with an IC50 of 12.9 µM. However, it did not inhibit PG. The potent antifungal and antitumor activities of the protein suggest that it can be developed into an antifungal agent for combating M. arachidicola invasion in crops and an agent for cancer therapy in humans.

Antifúngicos/isolamento & purificação , Fabaceae/química , Transcriptase Reversa do HIV/antagonistas & inibidores , Proteínas de Plantas/isolamento & purificação , Proteínas de Plantas/farmacologia , Inibidores da Transcriptase Reversa/isolamento & purificação , Sementes/química , Sequência de Aminoácidos , Antifúngicos/química , Antifúngicos/farmacologia , Antineoplásicos/química , Antineoplásicos/isolamento & purificação , Antineoplásicos/farmacologia , Linhagem Celular Tumoral , Proliferação de Células/efeitos dos fármacos , Fungos/efeitos dos fármacos , Humanos , Dados de Sequência Molecular , Proteínas de Plantas/química , Inibidores da Transcriptase Reversa/química , Inibidores da Transcriptase Reversa/farmacologia
Acta Biochim Pol ; 59(3): 407-12, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22946027


A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70°C. The enzyme activity increased steadily over the temperature range 20°C-70°C. There was only a slight reduction in activity at 80°C. However, all activity disappeared following exposure to 100°C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was undetectable at pH 8 and pH 9.

Proteínas Fúngicas/isolamento & purificação , Lacase/isolamento & purificação , Pleurotus/enzimologia , Adsorção , Sequência de Aminoácidos , Catecóis/química , Cromatografia DEAE-Celulose/métodos , Cromatografia em Gel/métodos , Eletroforese em Gel de Poliacrilamida/métodos , Ativação Enzimática , Ensaios Enzimáticos/métodos , Carpóforos/enzimologia , Proteínas Fúngicas/química , Concentração de Íons de Hidrogênio , Lacase/química , Peso Molecular , Fenilenodiaminas/química , Pirogalol/química , Análise de Sequência de Proteína/métodos , Especificidade por Substrato , Temperatura