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1. Effects of cadmium stress upon activities of antioxidative enzymes, photosynthetic rate, and production of phytochelatins in leaves and chloroplasts of wheat cultivars differing in yield potential

Creator:
Ahmad, I., Naeem, M., Khan, N. A., and Samiullah
Format:
bez média and svazek
Type:
model:article and TEXT
Subject:
ascorbate peroxidase, ATP-sulfurylase, catalase, glutathione, glutathione reductase, stomatal conductase, superoxide dismutase, Triticum, and water use efficiency
Language:
Multiple languages
Description:
We tested the mode of action of Cd on photosynthesis and activities of ATP-sulfurylase (ATP-S), catalase (CAT), superoxide dismutase (SOD), ascorbate peroxidase (APX), glutathione reductase (GR), and on contents of phytochelatins (PCs) and glutathione (GSH) in two cultivars of wheat (Triticum aestivum L.) PBW-343 and WH-542 differing in yield potential. Cd treatment increased Cd content and photosynthetic activity in PBW-343 more than in WH-542. The activities of APX, GR, ATP-S, and synthesis of PCs and GSH were also increased by Cd, but the CAT and SOD activities were inhibited in both the cultivars. The efficient functioning of antioxidative enzymes, production of PCs and GSH, helped in counteracting the effects of Cd namely in PBW-343, protected photosynthetic ability, and increased the tolerance to Cd. and I. Ahmad ... [et al.].
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public

2. Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro

Creator:
Tomáš Roušar, Patrik Pařík, Otto Kučera, Bartoš, M., and Zuzana Červinková
Format:
print
Type:
article, články, model:article, and TEXT
Subject:
Fyziologie člověka a srovnávací fyziologie, fyziologie, physiology, acetaminophen toxicity, glutathione reductase, glutathione, hepatotoxicity, 14, and 612
Language:
English
Description:
The aim of the present work was to investigate a new mechanism likely contributing to the toxic action of acetaminophen, especially to explore the possible inhibition of glutathione reductase through an acetaminophen-glutathione conjugate (APAP-SG). APAP-SG conjugate was synthesized by organic synthesis and purified by column chromatography. The inhibitory effect of the conjugate on two types of glutathione reductase (from yeasts and rat hepatocytes) was tested spectrophotometrically. We found that the enzyme activity was reduced similarly after the treatment with 2.96 mM acetaminophenglutathione conjugate in both yeast and hepatocyte glutathione reductases (GR); the enzyme activity was inhibited to 52.7±1.5 % (2.4±0.3 mU/ml) in yeast GR (control activity was 5.6±0.3 mU/ml) and to 48.1±8.8 % (2.2±0.2 mU/ml) in rat hepatocytes lysate GR (control activity was 5.2±0.2 mU/ml). In addition, the enzyme activity (from hepatocytes lysate) was decreased to 79±7 %, 67±2 % and 39±7 %, in 0.37, 1.48 and 3.7 mM concentration of the conjugate, respectively. We found that glutathione reductase, the essential enzyme of the antioxidant system, was dose-dependently inhibited by the product of acetaminophen metabolism - the conjugate of acetaminophen and glutathione., T. Roušar ... [et al.]., and Obsahuje bibliografii a bibliografické odkazy
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public