Relationship between the pentose phosphate shunt and methemoglobin reductase activity in human erythrocytes: Effect of aging on methemoglobin reductase activity.

The increase in methemoglobin reductase activity in human erythrocytes upon incubation with inosine, phosphate, pyruvate occurs only in the presence of methylene blue. No difference in activity of the methemoglobin reductases was observed between enzyme extracts of fresh cells and aged cells.     

Acceleration of methemoglobin reduction in erythrocytes by selenium

Summary Selenium accelerated the reduction of methemoglobin in erythrocytes. Its mode of action is suggested as a catalysis of the methemoglobin reduction by glutathione.     

Comparison of human adult and fetal hemoglobin: Aminophenol-induced methemoglobin formation

Summary Human fetal hemoglobin was more susceptible to methemoglobin formation in the presence of aminophenols than was adult hemoglobin. This was due to the intrinsic properties of the proteins rather than the presence of methemoglobin reductases.This work was supported by a grant from the National Institute of General Medical Sciences GM-17184.     

Stimulative effect of 2,3-diphosphoglycerate on methemoglobin reduction by ascorbic acid

Summary The reduction of methemoglobin by ascorbic acid was accelerated by the presence of 2,3-diphosphoglycerate     

Stimulation of methemoglobin reduction by selenium: a comparative study with erythrocytes of various animals

The extent of stimulation of methemoglobin (metHb) reduction by selenite depends upon the level of reduced glutathione (GSH) in the erythrocytes. The reason for the species difference in the effect of selenite was discussed with respect to species differences in the GSH levels in erythrocytes.     

Stimulation of methemoglobin reduction by selenium: A comparative study with erythrocytes of various animals

Summary The extent of stimulation of methemoglobin (metHb) reduction by selenite depends upon the level of reduced glutathione (GSH) in the erythrocytes. The reason for the species difference in the effect of selenite was discussed with respect to species differences in the GSH levels in erythrocytes.     

Methemoglobin in hypoxic rats

Methemoglobin levels have been found to vary with altitude and to shift the hemoglobin-oxygen dissociation curve. In this study, hematocrits and methemoglobin levels were monitored in rats exposed to hypoxia (420 torr absolute) for various intervals. Hematocrits gradually increased throughout the period of hypoxia, while methemoglobin levels rose by 12 h, peaked at 24 h and returned to control level by day 6. These data, in the context of other work, suggest that increased methemoglobin is important in acclimation to hypoxia.     

Effect of iron and hemoproteins on hydrogen peroxide-supported styrene oxidation to styrene oxide

Summary Fe²⁺, Fe³⁺ and their complexes with EDTA and hemin, methemalbumin and methemoglobin were active catalyzers of H₂O₂ supported styrene oxidation to styrene oxide. Methemoglobin was the most active compound; its peroxidative activity was comparable to that of cytochrome P-450 in liver microsomes of phenobarbital-treated rats. Cumene hydroperoxide supported styrene oxidation with methemoglobin and microsomal hemoproteins and was found to be more efficient than H₂O₂.This work was supported by C.N.R. (National Research Council) contract No. 79.03197.04.     

S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM(-1) min(-1), respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 microM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.     

Pyridoxine application enhances nitrate reductase activity and productivity ofVigna radiata

Summary Pyridoxine, applied to seeds before sowing or by the spraying of a standing crop of moong (Vigna radiata) significantly enhanced leaf nitrate reductase activity (NRA). Leaf NRA levels, being significantly correlated with seed yield, can be utilized for predicting crop productivity and for adopting corrective measures, if necessary, at an early growth stage.Acknowledgment. This work was partly supported by the award of a Research Fellowship to S.A.A. by the Government of India Council of Scientific and Industrial Research, New Delhi, which is gratefully acknowledged.     

Nitrate reductase activity in developing wheat ears

Zusammenfassung Die Fruchtstände der Weizenpflanzen reduzieren während ihrer Entwicklung beachtliche Mengen von Nitratstickstoff.     

Protective effect of selenite on nitrite toxicity.

Selenite was found to decrease nitrite-induced mortality in a dose-dependent manner. Its effect seems to be due to its action in reducing methemoglobin formed by nitrite.     

Rhythms of enzymatic activity in maternal and umbilical cord blood

The 24-h activity patterns of variouns enzymes were determined in human serum, red blood cells and white blood cells of maternal and umbilical cord blood. Blood was drawn from the brachial vein of mothers and from the umbilical cord within ten minutes after delivery. Corresponding blood specimens were obtained from 83 spontaneous labors, occurring at different hours over a period of 60 days. For each variable (variable=activity of a specific enzyme in one of the blood components) the results were grouped according to delivery hour, forming a 24-h pattern which was analyzed to elucidate time dependency. Five out of six corresponding maternal and fetal variables were similar with regard to pattern and peak time. The activity rhythms of glyceraldehyde-3-phosphate dehydrogenase and glucose phosphate isomerase in red blood cells of mothers and fetuses possessed a significant bimodal pattern. The activity rhythms of the latter enzyme in white blood cells and sera exhibited a significant 24-h period. Hexosaminidase activity exhibited a distinct 24-h rhythm in maternal white blood cells, but no significant rhythm could be detected in the fetal white blood cells. The activity of hexosaminidase showed, identical 24-h patterns in maternal and cord serum when analyzed by best fit cosine, and no significant time-dependency when analyzed by ANOVA.     

Protective effect of selenite on nitrite toxicity

Summary Selenite was found to decrease nitrite-induced mortality in a dose-dependent manner. Its effect seems to be due to its action in reducing methemoglobin formed by nitrite.     

Rhythms of enzymatic activity in maternal and umbilical cord blood.

The 24-h activity patterns of various enzymes were determined in human serum, red blood cells and white blood cells of maternal and umbilical cord blood. Blood was drawn from the brachial vein of mothers and from the umbilical cord within ten minutes after delivery. Corresponding blood specimens were obtained from 83 spontaneous labors, occurring at different hours over a period of 60 days. For each variable (variable = activity of a specific enzyme in one of the blood components) the results were grouped according to delivery hour, forming a 24-h pattern which was analyzed to elucidate time dependency. Five out of six corresponding maternal and fetal variables were similar with regard to pattern and peak time. The activity rhythms of glyceraldehyde-3-phosphate dehydrogenase and glucose phosphate isomerase in red blood cells of mothers and fetuses possessed a significant bimodal pattern. The activity rhythms of the latter enzyme in white blood cells and sera exhibited a significant 24-h period. Hexosaminidase activity exhibited a distinct 24-h rhythm in maternal white blood cells, but no significant rhythm could be detected in the fetal white blood cells. The activity of hexosaminidase showed, identical 24-h patterns in maternal and cord serum when analyzed by best fit cosine, and no significant time-dependency when analyzed by ANOVA.     

Superoxide dismutase activity decreases during erythrocyte aging

Summary Superoxide dismutase activity was determined by the adrenalin method in bovine erythrocytes separated according to age. Progressive loss of the enzyme activity was found, down to ca 65% of that of the youngest cells.     

Peroxidase activity in mitochondria of Prototheca moriformis

Summary Peroxidase activity was investigated by the use of diaminobenzidine method in fixed cells of Prototheca moriformis. A strong peroxidase activity was observed in the mitochondria. DAB staining was unaffected by KCN, aminotriazole and antimycin A, but it was completely inhibited by methanol-nitroferricyanide.     

Species-specific differences in the mitogenic activity of heparin-binding growth factors in the sera of various mammals

Sera from different mammalian species displayed great differences in mitogenic activity, as measured by stimulation of DNA synthesis in BALB/c 3T3 cells (3T3 cells). Among the sera examined, fetal bovine serum was least active, and increasing activity was detected in calf serum, human serum, rat serum and mouse serum, in that order. Rat and mouse sera exhibited extremely high mitogenic activity with 3T3 cells, but when TIG-1 human fetal lung fibroblasts were used for the DNA assay instead, the activity levels of all of the sera were lower, and the differences between them were smaller. To determine the reasons for these differences, the heparin-binding growth factors in each serum were separated on a heparin affinity column. Five peaks of DNA-stimulating activity were obtained. Three of these were found in all sera examined, with both 3T3 cells and TIG-1 cells. Two other peaks were found only with 3T3 cells; one was peculiar to rat and mouse sera, with extremely high activity in the rat, and the other was specific to fetal serum. The dependence of the activity of these peaks on the cells used for the test was confirmed using normal rat lung fibroblasts and immortalized rat kidney cells. These findings adequately explain the species-specific differences in mitogenic activity of whole sera, and the variation in activity depending on the cells used for assay of DNA synthesis.     

Erythrocyte NADH-methemoglobin reductase activity in experimental riboflavin deficiency

Zusammenfassung Bei Ratten mit Riboflavin-Mangel wurde eine normale Aktivität der NADH-abhängigen Methämoglobinreduktase festgestellt.