Inhibitory Effects of Licoisoflavones A and B and Sophoraisoflavone A of Sophra mooracroftiana BETH ex BAKER on Copper-Ion-Induced Protein Oxidative Modification of Mice Brain Homogenate, In Vitro

2001 ◽  
Vol 81 (2) ◽  
pp. 169-175 ◽  
Author(s):  
Shizuo Toda ◽  
Yoshiaki Shirataki
Keyword(s):  
Copper Ion ◽  
Brain Homogenate ◽  
Oxidative Modification ◽  
Inhibitory Effects ◽  
Protein Oxidative Modification ◽  
Mice Brain

scholarly journals Protein oxidative modification and cathepsin H activity in rats’ thymocytes at nitrogen oxide (II) synthesis modulation in vitro

2014 ◽  
Vol 95 (4) ◽  
pp. 553-557 ◽  
Author(s):  
Yu V Abalenikhina ◽  
M A Fomina
Keyword(s):  
Methyl Ester ◽  
Nitrogen Oxide ◽  
Nutrient Medium ◽  
No Synthase ◽  
Oxidative Modification ◽  
Control Group ◽  
Griess Reagent ◽  
Protein Oxidative Modification ◽  
Cathepsin H

Aim. To study the influence of substrate for nitrogen oxide (II) synthesis - L-arginine - and non-selective NO-synthase inhibitor - N-nitro-L-arginine-methyl ester - on protein oxidative modification in combination with rats’ thymocytes cathepsin H activity estimation in vitro. Methods. The study was performed on male Wistar rats with body weight of 280-320 g. Freshly-separated thymocytes were incubated in vitro in the full nutrient medium containing 5 мМ of N-nitro-L-arginine-methyl ester (n=8) or 5 мМ of L-arginine for 24 hours at the temperature of 37 °C (n=8). Control group consisted of thymocytes incubated in the same conditions in the full nutrient medium (n=8) for 24 hours. Nitric oxide metabolites levels were measured by spectrophotometry in the visible spectrum using the reaction with Griess reagent. Cathepsin H activity was estimated by BarrettKirschke spectrofluorimetry. Protein oxidative modification was measured by R.L. Levine method in E.E. Dubinina modification followed by carbonyl derivatives absorption spectrum quantitative analysis. Results. In nitrogen oxide (II) synthesis deficiency model, protein oxidative modification degree increased, mainly due to basic and neutral aldehyde- and ketone-dinitrophenylhydrazones level increase. Those changes were accompanied by increased activity of cathepsin H. In nitrogen oxide (II) synthesis stimulation model, level of oxidative-modified proteins decreased, mainly due to lower levels of neutral amino acid derivatives, cathepsin H activity didn’t change. Conclusion. In vitro nonselective inhibitor of inducible NO-synthase - N-nitro-L-arginine-methyl ester - stimulates protein oxidative modification and increases activity of cathepsin Н; substrate of NO synthesis - L-arginine - showes antioxidant effect.

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