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PubMed1987

Discomforts and laboratory findings in workers exposed to sulfur dioxide.

In a broom manufacturing factory the authors performed microclimatic measurements, measurements of sulfur dioxide concentration and dust content. Workers (n = 190) were polled regarding discomforts characteristic of sulfur dioxide effects. Sulfates were determined in urine of 56 subjects, and methemoglobin and sulfhemoglobin were determined in blood. Sulfates were determined in 43 controls and methemoglobin and sulfhemoglobin were determined in 39 controls. Sulfur dioxide concentration in work environment ranged from 17.1 to 149.4 mg/m3 in winter and from 0 to 0.75 mg/m3 in summer. The exposed workers complained most often of coughing (94.2%), dyspnea (91.0%), burning in nose, eyes and throat (from 74.7 to 83.7%), substernal pain (75.3%), sore throat (74.7%), tearing (64.7%), etc. Sulfate concentrations were found to be statistically significantly higher (P less than 0.01) in urine of workers exposed to sulfur dioxide than in the controls. Methemoglobin concentrations were also significantly higher in blood of the exposed workers, whereas no difference was found in concentrations of sulfhemoglobin.

Humans↗
PubMed1981

Ascorbate-cyanide test on red blood cells in uremia: effect of guanidinopropionic acid.

Red blood cells (RBC) of uremic or control subjects have been exposed to an oxidative stress by ascorbate and cyanide. The spectrophotometric determination of the sulfhemoglobin production has been used as a reliable method for the measurement of the hexose monophosphate shunt. The sulfhemoglobin production by RBC was significantly higher in uremic than in control subjects. Uremic plasma increased this production in uremic as well as in control RBC while control plasma was ineffective under the same conditions. In vitro the guanidinopropionic acid had the same toxic effect on normal RBC. These results suggest that the abnormal sulfhemoglobin production by uremic RBC might be due to an increased plasma concentration of guanidinopropionic acid in uremia.

Ascorbic Acid↗
PubMed1996

Hemoglobin oxidation products extract phospholipids from the membrane of human erythrocytes.

Hydrogen peroxide oxidation of human erythrocytes induces a transfer of phospholipid from the membrane into the cytosol [Brunauer, L.S., Moxness, M.S., & Huestis, W.H. (1994) Biochemistry 33, 4527-4532]. The current study examines the mechanism of lipid reorganization in oxidized cells. Exogenous phosphatidylserine was introduced into the inner monolayer of erythrocytes, and its distribution was monitored by microscopy and radioisotopic labeling. Pretreatment of cells with carbon monoxide prevented both hemoglobin oxidation and the transfer of phosphatidyserine into the cytosolic compartment. The roles of the various hemoglobin oxidation products in lipid extraction were investigated using selective oxidants. Nitrite treatment of intact cells produced almost complete conversion to methemoglobin, but no detectable lipid extraction. Treatments designed to produce the green hemoglobin derivatives, sulfhemoglobin and choleglobin, resulted in cytosolic extraction of phosphatidylserine. Ion exchange and size exclusion chromatography of oxidized cytosolic components revealed a lipid-hemoglobin complex. The interaction between lipid and hemoglobin oxidation products was verified in a model system. Purified hemoglobin, enriched in sulfhemoglobin and choleglobin by treatment with H2O2, H2S, or ascorbate, extracted phospholipid from small unilamellar phospholipid vesicles. Electron paramagnetic resonance studies demonstrated that hemoglobin oxidation products also adsorb fatty acids from solution. This newly described activity of hemoglobin may play a role in the clearance of oxidatively damaged and senescent cells from circulation.

Ascorbic Acid↗
PubMed1997

Protective effect of antioxidant vitamins on red blood cell lipoperoxidation induced by SO2 inhalation.

The aim of this research was to determine whether administration of antioxidant vitamins can reduce oxidant damage in erythrocytes induced by sulfur dioxide (SO2) inhalation. Meth- and sulfhemoglobin ratios, malonyldialdehyde (MDA) levels, osmotic fragility ratios and hematological parameters of a total of 28 rats were compared. SO2 was given at 10 ppm, 1 hour daily, for 45 days in a specially designed chamber. DL-alpha-Tocopherol acetate (40 mg/kg) and Na-ascorbate (200 mg/kg) treatments, initiated 3 days before SO2 exposures, were applied intraperitoneally 3 times a week for 45 days. Meth- and sulfhemoglobin ratios, MDA levels and osmotic fragility ratios were significantly higher in the SO2-treated group (p < 0.05). Significant decreases in MDA levels and osmotic fragility ratios were observed in the antioxidant-treated group (p < 0.05). SO2 inhalation resulted in higher MDA levels and osmotic fragility ratios, which can be reduced by vitamin E + C combination.

Air Pollutants↗
PubMed1975

Oxidative injury to erythrocytes, cell rigidity, and splenic hemolysis in hemodialyzed uremic patients.

In 23 hemodialyzed patients the metabolic defect of erythrocytes related to uremia and potentiated by dialysis was studied to establish a possible link with the shortened erythrocyte survival. A highly significant correlation was found between sulfhemoglobin provoked by oxidative stress and erythrocyte rigidity measured by filterability. Impaired filterability also correlated with the degree of splenic sequestration. Both sulfhemoglobin and impaired filterability correlated with the degree of hemolysis. Finally, erythrocyte survival showed a highly significant correlation with the degree of anemia. From osmotic fragility, plasma trapping, erythrocyte ATP and 2,3-diphosphoglycerate (DPG), and serum phosphorus, calcium, and magnesium measurements it seems unlikely that either spheric transformation or sol-gel transformation of the membrane is causing the increased erythrocyte rigidity. In view of the impaired erythrocyte defense capacity against oxidative injury, cell content rigidity as mediated by reduced hemoglobin solubility is a more likely explanation. Our results give a rational basis for a trial of splenectomy in severely anemia hemodialyzed patients.

Anemia, Hemolytic↗
PubMed1984

Determination of carboxyhemoglobin in the presence of other blood hemoglobin pigments by visible spectrophotometry.

The convenience of the spectrophotometric method for the determination of carboxyhemoglobin has been tempered by the observation that the analysis of postmortem bloods is often biased by the presence of pigments other than oxyhemoglobin, carboxyhemoglobin, and reduced hemoglobin. These other pigments include most prominently methemoglobin and sulfhemoglobin. Using a microprocessor-controlled spectrophotometer, a method was developed depending on absorbance difference measurements at isosbestic points for oxyhemoglobin, carboxyhemoglobin, and reduced hemoglobin that is accurate down to 2% carboxyhemoglobin in fresh blood. A correction for the error caused by methemoglobin is part of the method. Qualitative confirmation of carboxyhemoglobin by examination of spectra details, sodium dithionite reduction, and first derivative spectra is described. The analysis of denatured and autolyzed bloods is examined in the context of postmortem case reports. A number of spectra are shown in detail, including methemoglobin, sulfhemoglobin, alkaline hematin, acid hematin, and mixtures of blood pigments containing varying concentrations of carboxyhemoglobin. The method has been shown to be precise, accurate, and reliable for fresh bloods. While accuracy for denatured bloods is diminished, reliability of carboxyhemoglobin identification is maintained. The analysis time is about 5 min for routine blood samples and the method is easily implemented with a precise microprocessor-controlled spectrophotometer.

Carboxyhemoglobin↗
PubMed2002

Blood parameters and metabolites in the teleost fish Colossoma macropomum exposed to sulfide or hypoxia.

Juvenile tambaqui, Colossoma macropomum, were exposed to sulfide and hypoxia for 12, 24, 48 and 96 h. Hemoglobin concentrations, red blood cell counts, and mean cell hemoglobin, were higher at 12 h in fish exposed to hypoxia. However, control fish and those exposed to sulfide and hypoxia had lower red blood cell count, hemoglobin concentration and hematocrit at 96 h. Methemoglobin was higher than in the controls, probably due to the hypoxemia induced by these stressors. Sulfhemoglobin was not detected in significant amounts in the blood of fish exposed to sulfide (in vivo), yet hemoglobin converted into sulfhemoglobin at 1-15 mM sulfide in vitro. Anaerobic metabolism seemed to be an important mechanism for adapting to sulfide exposure and blood pH returned to control values after 24 h of sulfide, preventing acidosis. The high sulfide tolerance in tambaqui is associated with its high tolerance to hypoxia.

Animals↗
PubMedDate not supplied

Topical anesthetic-induced methemoglobinemia and sulfhemoglobinemia in macaques: a comparison of benzocaine and lidocaine.

Benzocaine (BNZ) and lidocaine (LC) are commonly used topical (spray) anesthetics approved for use in humans. Benzocaine has structural similarities to methemoglobin (MHb)-forming drugs that are current candidates for cyanide prophylaxis, while LC has been reported to increase MHb in man. In this study, we compared MHb and sulfhemoglobin (SHb) production in three groups of Macaques (Chinese rhesus and Indian rhesus (Macaca mulatta) and pig-tailed macaques (Macaca nemestrina)) after exposure to BNZ and LC. Formation of SHb, unlike MHb, is not thought to be reversible and therefore is considered to be of greater toxic significance. Both MHb and SHb levels were measured periodically on a CO-Oximeter. All rhesus macaques (n = 8) were administered an intratracheal/intranasal) dose of 56 mg (low dose) or 280 mg (high dose) of BNZ or 40 mg of LC in a randomized cross-over design (all animals received all three treatments). Pig-tailed macaques (n = 6) were given an intranasal dose of 56 mg of BNZ and 40 mg of LC. As no differences in the peak MHb or time to peak (mean +/- SD) were observed among the three macaque subspecies, the data were pooled. Lidocaine did not cause MHb or SHb formation above baseline in any monkey. In contrast, all monkeys (n = 14) had a significant elevation in peak MHb formation after 56 mg of BNZ, which ranged from 4.0% to 19.4% with an average of 8.6 +/- 4.0% (mean +/- SD), with peak MHb levels reached at 30 min.(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Intranasal↗
PubMed1975

The demonstration of ferrihemochrome intermediates in heinz body formation following the reduction of oxyhemoglobin A by acetylphenylhydrazone.

Interaction of acetylphenylhydrazine with oxyhemoglobin A in a hemolysate or in intact red cells resulted in the formation of ferrihemochromes as shown by a characteristic optical spectrum. The same optical spectrum was observed in a suspension of red cell ghosts containing numerous Heinz bodies. Electron paramagnetic resonance of actylphenylhydrazine-incubated red cells disclosed the presence of previously identified reversible ferrihemochromes, which can be reduced to functional hemoglobin, and irreversible ferrihemochromes, which cannot be reduced to functional hemoglobin. (Ferrihemochromes are defined as low spin forms of ferric hemoglobin having heme ligands endogenous to the protein structure). In contrast, only irreversible ferrihemochromes could be observed in ghosts containing Heinz bodies. In addition both optical and magnetic features of sulfhemoglobin were observed in an acetylphenylhydrazine-treated red cell hemolysate. Similar optical features are produced by the interaction of aromatic nitrogen-containg reductants with purified oxyhemoglobin in the presence of (NH4)2S. This reaction is not effected by the presence of catalase, suggesting that H2O2 is not an intermediate of the reaction. It is concluded that the mechanism of action of acetylphenylhydrazine with oxyhemoglobin is two-fold, ultimate reduction to high spin ferric hemoglobin followed by ferrihemochrome formation. Thus it appears that the pathway of denaturation of hemolytic anemias and thalassemia or induced by chemical reagents, entails a common route involving the formation of ferric hemoglobin by a reductive mechanism, followed by reversible ferrihemochromes, irreversible ferrihemochromes, and ultimately, precipitation.

Chemical Phenomena↗
PubMed1987

Diode-array spectrophotometry for simultaneous measurement of hemoglobin pigments.

A prototype oxygen saturation meter was used to measure the concentrations of deoxygenated hemoglobin (rHb), oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), methemoglobin (MetHb), and sulfhemoglobin (SHb) in 35 microliter blood. Simultaneous absorbance measurements at 535, 560, 577, 622, 636, and 670 nm permitted the composition of any hemoglobin pigment mixture to be determined more accurately, precisely and easily than before. The inclusion of 670 nm, where the hemoglobin pigments have low absorption coefficients, allowed correction for turbidity.

Adult↗
PubMed1985

Green pigments in epidermal blisters of decomposed cadavers.

A spectrophotometrical method for discrimination between sulfhemoglobin (SHb) and choleglobin was applied to analyses of the green pigments in epidermal blisters of decomposed cadavers. SHb appeared to be a predominant constituent of the pigments, although significant amounts of choleglobin, one third to one sixth of SHb, were also demonstrated. The present results indicate that the greenish discoloration of decomposed cadavers is due to formation of a mixture of SHb, choleglobin and possibly other denatured hemoglobin derivatives.

Blister↗
PubMedDate not supplied

[Study of hemoglobin system components and antioxidation enzymes in cadmium intoxication].

Cadmium intoxication has been defined to make material changes in hemoglobin system by elevation of sulfhemoglobin and methhemoglobin levels on the back-cloth of lowering of general hemoglobin. Alongside with the latter there is observed a violation of antioxydation protection including the activity of erythrocytic catalase, ceruloplasmin, ferrum saturation of transferrine.

Animals↗
PubMed1988

Performance of an automated six-wavelength photometer (Radiometer OSM3) for routine measurement of hemoglobin derivatives.

A new instrument for spectrophotometric determination of oxygen saturation (SO2) and the fractions of carboxyhemoglobin (FHbCO) and methemoglobin (FHi), the Hemoximeter OSM3 (Radiometer), was tested by comparative measurements with a multiwavelength method. We found that it gave reliable results for freshly drawn samples from patients. When samples with artificially induced high proportions of HbCO or Hi, or both, were introduced, results were still sufficiently accurate. The presence of sulfhemoglobin (SHb) seriously interfered with the measurement of SO2, FHbCO, and FHi, but the instrument reliably indicated its presence. Because SHb is rarely encountered, a reliable warning for its presence is adequate for clinical practice. Using the instrument in its fetal mode, we obtained accurate results for blood samples from newborns.

Adult↗
PubMed1986

Results of routine determination of clinically significant hemoglobin derivatives by multicomponent analysis.

Our recently developed multiwavelength method for multi-component analysis of hemoglobin (Hb) derivatives (Clin Chem 1984;30:373-379) was adapted for routine use in the clinical chemical laboratory. The method was applied in 4066 determinations on blood specimens from patients awaiting major surgery (n = 3863) or visiting the outpatient department for pulmonary disease (n = 203). Mean total hemoglobin concentration was 141 (SD 14) g/L. The proportion of HbCO was slightly to moderately increased (1.5-10.0%) in 36.5% of all patients; in a few cases it was as high as 15%. Mean methemoglobin was 0.4% (SD 0.2%) in the surgical patients, but 1.5% (SD 0.8%) in the patients with pulmonary disease. In some patients of the latter group the proportion of methemoglobin amounted to 5%. Sulfhemoglobin was found less than 0.4% in all specimens. Interference by paraproteins and by increased concentrations of bilirubin and lipids in plasma was easily detected by means of the performance checks provided by the spectrophotometer (an HP 8451 UV/Vis). The method is equally suitable for measuring blood samples containing fetal hemoglobin.

Adolescent↗
PubMed1995

The effects of sulfur dioxide inhalation and antioxidant vitamins on red blood cell lipoperoxidation.

An attempt was made to determine whether sulfur dioxide (SO2,) inhalation at 10 ppm, 1 hr daily, for 30 days induces oxidant stress and whether vitamin E (40 mg/kg) together with vitamin C (200 mg/kg), administered intraperitoneally once in every 3 days, can reduce the damage in red blood cell membranes of guinea pigs. Malonyldialdehyde (MDA) levels, osmotic fragility ratios, and methemoglobin and sulfhemoglobin values were significantly higher in the SO2-treated group compared with the control group (P < 0.05), and marked decreases in MDA levels and osmotic fragility ratios were determined in the group treated with SO2 + antioxidant vitamins (P < 0.05).

Administration, Inhalation↗
PubMed1976

Isoelectrofocusing: a method of multiple applications for hemoglobin studies.

A microanalytical screening of hemoglobins by isoelectric focusing on acryl-amide gel columns is described. Addition of this technique to our regular analytical procedures revealed many mutants, praticularly some neutral ones which were not resolved by other conventional procedures. Extension of this technique to a quantitative scale permitted rapid isolation of some unstable mutants in an almost pure form ready for functional studies. The natural color of the separated components is often indicative of their nature and in cases like the sulfhemoglobin, Hbs M, they are of diagnostic value. The heme-losing, abnormal, unstable mutants, on the addition of external cyanhemin, take them up and change their isoelectric pH. This is an attractive visible procedure for their diagnosis. From all these results, it appears that isoelectric focusing as a single method brings more information than the other conventional procedures and hence can be considered as a semi-routine investigation for hemoglobin studies before deciding on a much longer procedure.

Fetal Hemoglobin↗
PubMed1989

Inactivation of intracellular copper-zinc superoxide dismutase by copper chelating agents without glutathione depletion and methemoglobin formation.

The copper chelator N,N'-diethyldithiocarbamate (DDC), is often used to inactivate intracellular copper-zinc superoxide dismutase in erythrocytes. However, in studies with red cells we found that the compound also reacted with oxyhemoglobin to produce oxygen radicals in addition to generating lipid peroxidation products, oxidized N,N'-diethyldithiocarbamate, methemoglobin, and sulfhemoglobin. Moreover, intracellular glutathione was depleted and vital cellular enzymes were susceptible to inactivation. We, and others, have confirmed these findings in nonerythrocytic cell lines. Thus, cells exposed to DDC are severely damaged before studies on the effects of added putative superoxide producing compounds can be performed with them. In this report, we have systematically investigated other copper chelators for their ability to inactivate intracellular copper-zinc superoxide dismutase without producing the deleterious effects mentioned above. Catechol, triethylenetetramine, and tetraethylenepentamine were found to be such agents when erythrocytes were dialyzed in the cold against dilute solutions of these chelators. In addition, with a myeloid leukemic cell line (HL-60), triethylenetetramine inhibited SOD without causing significant GSH oxidation. Examination of the affinity constants of chelators active against purified copper-zinc superoxide dismutase indicated that an affinity binding constant (log K1) between 12.6 and 13.8 was required for the chelator to successfully remove copper from the enzyme.

Cell Line↗
PubMed2004

Physiological responses to sulfide toxicity by the air-breathing catfish, Hoplosternum littorale (Siluriformes, Callichthyidae).

Hemolytic anemia accompanied by changes in the immunology system is one of the sulfide intoxication harmful effects on Hoplosternum littorale. Hematological parameters are considered as effective indicators of stress caused by this hydrogen sulfide. During sulfide exposure, H. littorale neither alters the methemoglobin concentration nor forms sulfhemoglobin in the presence of high levels of dissolved sulfide in the water. Cytochrome c oxidase shows little activity in the gills and blood of H. littorale when exposed to sulfide. Alternative metabolic routes are suggested through which the accumulation of pyruvate leads to the formation of an end product other than lactate.

Animals↗