METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (6) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

Effects of hydrogen peroxide on the responsiveness of isolated canine bronchi: role of prostaglandin E2 and I2

1992 ◽  
Vol 263 (3) ◽  
pp. L402-L408 ◽  
Author(s):  
Y. Gao ◽  
P. M. Vanhoutte
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Smooth Muscle ◽  
Prostaglandin E2 ◽  
Respiratory Epithelium ◽  
Isometric Tension ◽  
Third Order ◽  
Bronchial Smooth Muscle ◽  
Cyclic Monophosphate

The present study was design to determine the role of prostaglandin E2 and I2 in the responses of isolated canine airways to H2O2. Rings of canine third-order bronchi, some of which had undergone mechanical denudation of the epithelium, were suspended in organ chambers; isometric tension was recorded. During contractions to acetylcholine, H2O2 induced concentration-dependent relaxations. The relaxations were attenuated significantly by indomethacin, acetylsalicylic acid, and methylene blue. H2O2 increased the release of prostaglandin E2 and 6-keto-prostaglandin F1 alpha and the content of adenosine 3',5'-cyclic monophosphate (cAMP). These effects were abolished by indomethacin or methylene blue. H2O2 did not affect the content of guanosine 3',5'-cyclic monophosphate significantly. These observations suggest that 1) H2O2 relaxes canine bronchial smooth muscle and 2) elevation of tissue content of cAMP induced by prostaglandin E2 and I2 may be involved. These phenomena did not appear to be modulated by the respiratory epithelium, since H2O2-induced relaxations and increases in the release of PGE2 and 6-ketoprostaglandin F1 alpha were similar in preparations with and without epithelium. However, after treatment with methylene blue, H2O2 induced contractions only in preparations with epithelium. These epithelium-dependent contractions were not affected by inhibitors of cyclooxygenase and lipoxygenase.

The role of malate in nitrate reduction in spinach leaves

1980 ◽  
Vol 58 (5) ◽  
pp. 517-521 ◽  
Author(s):  
K. C. Woo ◽  
D. T. Canvin
Keyword(s):  
Nitrate Reduction ◽  
Nitrite Accumulation ◽  
Antimycin A ◽  
Anaerobic Conditions ◽  
Aerobic Conditions ◽  
Leaf Discs ◽  
Spinach Leaf ◽  
Spinach Leaves

In spinach leaf discs the accumulation of nitrite from nitrate reduction under anaerobic conditions in the light in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) was inhibited by air. The inhibition of nitrate reduction by air was reversed by antimycin A but not by rotenone or amytal. The nitrate-reducing system of DCMU-inhibited leaf discs in the light appeared similar to noninhibited leaf discs in the dark. In aerobic conditions, the addition of malate stimulated nitrite accumulation. This stimulation was unaffected by malonate. Under anaerobic conditions, malate reversed the inhibition of nitrate reduction caused by either iodoacetate or arsenite to rates similar to those observed in the dark and in the light with DCMU. Malate can apparently provide a direct source of cytosolic NADH for nitrate reduction.

Metabolic activities of sheep erythrocytes. II. Formate metabolism

1962 ◽  
Vol 13 (1) ◽  
pp. 45 ◽  
Author(s):  
RA Leng ◽  
EF Annison
Keyword(s):  
Carbon Dioxide ◽  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Aerobic Oxidation ◽  
Carbon Dioxide Production ◽  
Anaerobic Conditions ◽  
Formate Oxidation ◽  
Metabolic Activities ◽  
Sulphydryl Compounds ◽  
Formate Metabolism

Whole sheep blood, washed erythrocytes, and haemolysates showed only a slight capacity to oxidize 14C-labelled formate, as measured by labelled carbon dioxide production. Considerable oxidation of formate by washed erythrocytes or haemolysates occurred in the presence of systems generating hydrogen peroxide enzymically or non-enzymically under aerobic conditions. In addition, methylene blue was found to stimulate markedly the aerobic oxidation of formate by erythrocytes and haemolysates, the effect being abolished under anaerobic conditions. The stimulatory effects of methylene blue and sulphydryl compounds were additive. Evidence was obtained that the effect of methylene blue was mediated through an enzyme which directly or indirectly gave rise to hydrogen peroxide, formate oxidation being achieved by a hydrogen peroxide-catalase complex. No evidence was obtained of formate incorporation into red cells.

scholarly journals Exposure of erythrocytes to methylene blue shows the active role of catalase in removing hydrogen peroxide

2002 ◽  
Vol 119 (3) ◽  
pp. 833-838 ◽  
Author(s):  
Gian Franco Gaetani ◽  
Davide Rapezzi ◽  
Rosa Mangerini ◽  
Omar Racchi ◽  
Michela Rolfo ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Active Role

A novel nanoplatform encapsulating glucose oxidase for spectrophotometric biosensing of hydrogen peroxide and glucose

2020 ◽  
Vol 12 (3) ◽  
pp. 345-357
Author(s):  
Hamzeh Pezhhan ◽  
Morteza Akhond ◽  
Mojtaba Shamsipur
Keyword(s):  
Hydrogen Peroxide ◽  
Glucose Oxidase ◽  
Protein Interactions ◽  
Magnetic Nanoparticle ◽  
Marine Mussels

Inspired by the role of the chelation of Fe3+–catechol in inter-protein interactions and the production of adhesives by marine mussels, we used DA as an anchor to connect GOx to Fe3O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells.

scholarly journals Management of environmental analysis waste using Fenton-type oxidation processes

2019 ◽  
Author(s):  
William Bardelin Nunes ◽  
Enelton Fagnani ◽  
Renato F. Dantas
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Environmental Analysis ◽  
Advanced Oxidation Processes ◽  
Methyl Red ◽  
Oxidation Processes ◽  
No Formation ◽  
Degradation Of Dyes ◽  
Ph Conditions

The management of environmental analysis waste through Fenton-based advanced oxidation processes is proposed. Degradation of dyes as methylene blue (MB) and methyl red (MR) is obtained in presence of iron(II)-complex and hydrogen peroxide at mildly pH conditions with no formation of sludge. The role of temperature and UV-A are discussed.

Susceptibility to hydrogen peroxide ofPlasmodium falciparuminfecting glucose-6-phosphate dehydrogenase-deficient erythrocytes

Parasitology ◽  
1989 ◽  
Vol 99 (2) ◽  
pp. 171-174 ◽  
Author(s):  
S. Kamchonwongpaisan ◽  
A. Bunyaratvej ◽  
W. Wanachiwanawin ◽  
Y. Yuthavong
Keyword(s):  
Hydrogen Peroxide ◽  
Plasmodium Falciparum ◽  
Glucose Oxidase ◽  
Host Cells ◽  
Parasite Invasion ◽  
Killing Effect ◽  
Oxidase System ◽  
Relative Susceptibility ◽  
Glucose 6 Phosphate Dehydrogenase

SummaryThe susceptibility to oxidant-mediated killing ofPlasmodium falciparuminfecting normal and glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes was assessed by exposure to hydrogen peroxide generated by the glucose–glucose oxidase system. The parasites infecting G6PD-deficient erythrocytes had markedly greater susceptibility to hydrogen peroxide under a variety of conditions than those infecting normal erythrocytes. In both cases, the killing effect was mediated mainly through the host cells since treatment of the erythrocytes with hydrogen peroxide did not change their relative susceptibility. The parasites were most susceptible during maturation, especially in G6PD-deficient erythrocytes, although a reduction in parasite invasion was also observed. The role of oxidant-mediated killing in the protection of G6PD-deficient hosts fromP. falciparuminfection is discussed.

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