scholarly journals Inhibitory effect of retinol acetate on horseradish peroxidase

2013 ◽  
Vol 67 (3) ◽  
pp. 419-426
Author(s):  
Vladan Djuric ◽  
Nebojsa Deletic ◽  
Vesna Stankov-Jovanovic ◽  
Ranko Simonovic
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Enzymatic Reaction ◽  
Inhibitory Effect ◽  
Enzyme Concentration ◽  
Water Soluble ◽  
Primary Role ◽  
Retinol Acetate ◽  
Peroxidase Enzyme

Primary role of peroxidase enzyme is to decompose endogenous hydrogen peroxide, when oxygen radical is being replaced by a less potent radical, which is its cosubstrates oxidized form. During this study, catalytic activity of horseradish peroxidase has been observed in the presence of antioxidants from vitamin group, such as C, E and A, i.e. their water-soluble forms. It was found that vitamin E showed no effect on the enzyme activity and fate of cosubstrate radicals from the group of benzidine derivatives. Vitamin C proceeds enzymatic reaction showing its antioxidative character, and absorbs electrons from radicals, bringing cosubstrate back to its relaxed state. On the other hand, vitamin A plays a role of uncompetitive peroxidase inhibitor, which is visible through decreasing initial rate of catalytic reaction, and is reflected as virtual decrease of enzyme concentration. Furthermore, it prolongs life of endogenous hydrogen peroxide, which could potentially lead to oxidative stress of cells. This inhibitory effect can be used in analytical purpose, for determination of retinol acetate content in a sample.

Role of 2,4-Dichlorophenol in the Oxidation of Estradiol by Uterine and Horseradish Peroxidase

1973 ◽  
Vol 51 (7) ◽  
pp. 1066-1071 ◽  
Author(s):  
C. R. Lyttle ◽  
T. McNabb ◽  
P. H. Jellinck
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Water Soluble

The role of 2,4-dichlorophenol in enhancing the conversion of [4-14C]estradiol to water-soluble products by a uterine preparation in the presence of hydrogen peroxide has been investigated. The addition of this phenol to a solution of uterine or horseradish peroxidase in 8 M urea restored the activity of the enzyme and also that of horseradish peroxidase inactivated by heating. It also protected the enzyme from inactivation during incubation. It is proposed that 2,4-dichlorophenol exerts its effect by activating peroxidase and protecting the enzyme from inactivation by the products of the reaction.

Role of peroxidase and chitosan in removing chlorophenols from aqueous solution

1996 ◽  
Vol 34 (10) ◽  
pp. 151-159 ◽  
Author(s):  
Hossein Ganjidoust ◽  
Kenji Tatsumi ◽  
Shinji Wada ◽  
Mitsuo Kawase
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Peroxide ◽  
Reaction Time ◽  
Horseradish Peroxidase ◽  
Industrial Wastewater ◽  
Aluminum Sulfate ◽  
Enzymatic Reaction ◽  
Hexamethylene Diamine ◽  
Natural Coagulant

Chlorophenols removal from industrial wastewater by horseradish peroxidase and coagulant was investigated. It was found that an enzymatic reaction time of less than one hour was enough for the reaction to reach 95% completion. Chitosan, which is a natural coagulant, was an effective coagulant as compared to mineral coagulants such as aluminum sulfate (ALUM), hexamethylene diamine epichlorohydrin polycondensate (HX), polyacrylamide (PAM), and polyethyleneimine (PEI). A combination of 0.4 U/mL peroxidase to 2 ppm chitosan along with 0.8 mM of hydrogen peroxide resulted in over 95% chlorophenol removal from aqueous solution.

scholarly journals Decolorization of Anthraquinonic Dyes from Textile Effluent Using Horseradish Peroxidase: Optimization and Kinetic Study

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Nataša Ž. Šekuljica ◽  
Nevena Ž. Prlainović ◽  
Andrea B. Stefanović ◽  
Milena G. Žuža ◽  
Dragana Z. Čičkarić ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Treatment Time ◽  
Substrate Inhibition ◽  
Oxygen Demand ◽  
Enzyme Concentration ◽  
Influence Of Process Parameters ◽  
Peroxidase Enzyme ◽  
Acid Blue ◽  
Acid Violet

Two anthraquinonic dyes, C.I. Acid Blue 225 and C.I. Acid Violet 109, were used as models to explore the feasibility of using the horseradish peroxidase enzyme (HRP) in the practical decolorization of anthraquinonic dyes in wastewater. The influence of process parameters such as enzyme concentration, hydrogen peroxide concentration, temperature, dye concentration, and pH was examined. The pH and temperature activity profiles were similar for decolorization of both dyes. Under the optimal conditions, 94.7% of C.I. Acid Violet 109 from aqueous solution was decolorized (treatment time 15 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.4 mM, dye concentration 30 mg/L, pH 4, and temperature 24°C) and 89.36% of C.I. Acid Blue 225 (32 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.04 mM, dye concentration 30 mg/L, pH 5, and temperature 24°C). The mechanism of both reactions has been proven to follow the two substrate ping-pong mechanism with substrate inhibition, revealing the formation of a nonproductive or dead-end complex between dye and HRP or between H2O2and the oxidized form of the enzyme. Both chemical oxygen demand and total organic carbon values showed that there was a reduction in toxicity after the enzymatic treatment. This study verifies the viability of use of horseradish peroxidase for the wastewaters treatment of similar anthraquinonic dyes.

scholarly journals Role of Hydrogen Peroxide in the Inhibitory Effect of Ascorbate on Cell Growth.

1994 ◽  
Vol 40 (3) ◽  
pp. 219-227 ◽  
Author(s):  
Nobuhiko ARAKAWA ◽  
Shino NEMOTO ◽  
Emiko SUZUKI ◽  
Megumi OTSUKA
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Growth ◽  
Inhibitory Effect

scholarly journals THE RELATIONSHIP OF HYDROGEN PEROXIDE TO THE INHIBITION OF THE GLYOXALASE ACTIVITY OF INTACT ERYTHROCYTES BY X-RADIATION

1958 ◽  
Vol 41 (4) ◽  
pp. 737-753 ◽  
Author(s):  
S. J. Klebanoff
Keyword(s):  
Hydrogen Peroxide ◽  
Plasma Glucose ◽  
Physiological Saline ◽  
Inhibitory Effect ◽  
Enzyme Systems ◽  
Low Concentrations ◽  
X Irradiation ◽  
Ionizing Radiations ◽  
Relationship Of

The x-irradiation of a dilute suspension of erythrocytes results in a decrease in the glyoxalase activity of the cells as a result of a fall in the reduced glutathione level. The present paper deals with the possible role of H2O2 in this reaction. The addition of intact erythrocytes to physiological saline previously irradiated with 150,000 r or 225,000 r results in a fall in the glyoxalase activity of the cells. The inhibition is prevented by the preincubation of the irradiated saline with catalase and is reversed by the addition of plasma, glucose, adenosine, and inosine to the cell suspension. An inhibition of the glyoxalase activity is also produced by the addition of H2O2 to the suspension of erythrocytes. The inhibitory effect of H2O2 can be prevented and largely reversed by plasma, glucose, adenosine, and inosine. Methylglyoxal is also protective under these conditions. Hydrogen peroxide formed continuously and in low concentrations by enzyme systems appears to be more effective than added H2O2 in inhibiting the glyoxalase system. The inhibition by H2O2-producing enzyme systems is minimized by the addition of catalase, plasma, glucose, methylglyoxal, and to a lesser extent, by adenosine and inosine, and is accentuated by the addition of sodium azide. The results are discussed in relation to the role of H2O2 and catalase in the toxicity of ionizing radiations.

The role of Arginine 38 in horseradish peroxidase enzyme revisited: A computational investigation

2009 ◽  
Vol 141 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Simone Tatoli ◽  
Costantino Zazza ◽  
Nico Sanna ◽  
Amedeo Palma ◽  
Massimiliano Aschi
Keyword(s):  
Horseradish Peroxidase ◽  
Computational Investigation ◽  
Peroxidase Enzyme

Enzyme catalyzed polymerization and precipitation of aromatic compounds from aqueous solution

1993 ◽  
Vol 20 (5) ◽  
pp. 725-735 ◽  
Author(s):  
J. A. Nicell ◽  
J. K. Bewtra ◽  
N. Biswas ◽  
C. C. St. Pierre ◽  
K. E. Taylor
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Aromatic Compounds ◽  
Thermal Inactivation ◽  
Catalytic Efficiency ◽  
Reaction Products ◽  
Aromatic Substrate ◽  
Aromatic Substrates ◽  
Minimum Residual ◽  
Peroxidase Enzyme

Horseradish peroxidase enzyme (HRP), once activated by hydrogen peroxide, initiates the oxidation of a wide variety of aromatic compounds. Reaction products undergo a non-enzymatic polymerization to form water insoluble aggregates which are readily separated from solution. HRP was selected for application in wastewater treatment systems due to its stability and retention of its catalytic ability over wide ranges of pH and temperature. HRP activity was optimal between pH 5.7 and 8.5 with peak activity occurring at neutral pH. Activity increased with temperature up to 50 °C and declined at higher temperatures due to thermal inactivation. HRP was inactivated rapidly by hydrogen peroxide in the absence of an aromatic substrate. The efficiency of removal that was achieved was dependent on the nature of the aromatic undergoing treatment and the amount of enzyme provided due to the finite lifetime of the catalyst. Optimization of pH significantly improved catalytic efficiency with a corresponding savings in treatment costs. Optimal catalytic lifetime of HRP was achieved in the pH range of 7 to 9 for the eight phenolic compounds treated. The minimum residual level to which aromatic substrates were removed from solution was independent of the starting concentration of the aromatic substrate. Enhanced removal of hard-to-remove compounds was noted when mixtures of aromatic substrates were treated. Key words: horseradish peroxidase enzyme, polymerization, wastewater, phenols, aromatics amines.

scholarly journals Hydrogen peroxide inhibits non-small cell lung cancer cell anoikis through the inhibition of caveolin-1 degradation

2011 ◽  
Vol 300 (2) ◽  
pp. C235-C245 ◽  
Author(s):  
Pimuma Rungtabnapa ◽  
Ubonthip Nimmannit ◽  
Hasseri Halim ◽  
Yon Rojanasakul ◽  
Pithi Chanvorachote
Keyword(s):  
Hydrogen Peroxide ◽  
Cancer Cell ◽  
Negative Regulator ◽  
Ros Generation ◽  
Cell Detachment ◽  
Primary Role ◽  
Major Pathway ◽  
Caveolin 1 ◽  
Human Lung Carcinoma

Anoikis or detachment-induced apoptosis plays an essential role in the regulation of cancer cell metastasis. Caveolin-1 (Cav-1) is a key protein involved in tumor metastasis, but its role in anoikis and its regulation during cell detachment are unclear. We report here that Cav-1 plays a key role as a negative regulator of anoikis through a reactive oxygen species (ROS)-dependent mechanism in human lung carcinoma H460 cells. During cell detachment, Cav-1 is downregulated, whereas ROS generation is upregulated. Hydrogen peroxide and hydroxyl radical are two key ROS produced by cells during detachment. Treatment of the cells with hydrogen peroxide scavengers, catalase and N-acetylcysteine, promoted Cav-1 downregulation and anoikis during cell detachment, indicating that produced hydrogen peroxide plays a primary role in preventing anoikis by stabilizing Cav-1 protein. Catalase and N-acetylcysteine promoted ubiquitination and proteasomal degradation of Cav-1, which is a major pathway of its downregulation during cell anoikis. Furthermore, addition of hydrogen peroxide exogenously to the cells inhibited Cav-1 downregulation by preventing the formation of Cav-1-ubiquitin complex, supporting the inhibitory role of endogenous hydrogen peroxide in Cav-1 degradation during cell detachment. Together, these results indicate a novel role of hydrogen peroxide as an endogenous suppressor of cell anoikis through its stabilizing effect on Cav-1.

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