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Activity of lysosomal enzymes in acute intoxication with organophosphorus insecticides

100%

Lukaszewicz-Hussain A., Moniuszko-Jakoniuk J.

Polish Journal of Environmental Studies

1997

tom 06

nr 1

The aim of this paper was to examine the activity of lysosomal enzymes after intoxication with chlorfenvinvos and dichlorvos - phosphoorganic insecticides. Investigations were carried out on male Wistar rats weighing 180-230 g. Rats were divided into two groups: control and treated. Rats of treated group were receiving oil solution of chlorfenvinvos at doses of 0.5 LD50 or 0.1 LD5(), determinations were performed after 1 and 24 hours after treatment or dichlorvos in the dose equal to 0.5 LD50 estimations were performed after 1 h only. Rats of control group were given equivalent volume of oil. Activities of beta-glucuronidase and acid phosphatase in the blood serum and lysosomal fraction of rat liver homogenate were determined. It was found that the level of ChE inhibition and increase of BGR activity in the serum were dependant on chemical structure of used compound, dose and time after treatment. It was observed that increase of hydrolases activities in serum was accompanied by the decrease in its activity in the lysosomal fraction of liver homogenate.

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

84%

Sun J., Zhao Y., Chai H., Wang H., Ng T. B.

Acta Biochimica Polonica

2011

tom 58

nr 4

A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Polish Journal of Environmental Studies

1 Chai H.

1 Lukaszewicz-Hussain A.

1 Moniuszko-Jakoniuk J.

1 Ng T. B.

1 Sun J.

1 Wang H.

1 Zhao Y.

1 2011

1 1997

Wyniki wyszukiwania

Activity of lysosomal enzymes in acute intoxication with organophosphorus insecticides

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa