PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Sulfhemoglobin”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1978

The reversible binding of oxygen to sulfhemoglobin.

The O2 binding properties of sulfhemoglobin were studied. The oxygen tension required for half-saturation of sulfhemoglobin is more than 2 orders of magnitude higher than that for hemoglobin A. The binding of O2 exhibits an alkaline Bohr effect larger than that observed for hemoglobin, yet the Hill number is unity. From the Bohr titration curve, 0.68 proton is released during O2 binding at 0 degrees C. Sulfhemoglobin prepared from carboxypeptidase A-treated hemoglobin has an affinity for O2 which is about the same as that of sulfhemoglobin at the theoretical limit of the Bohr titration curve. Like its carboxypeptidase A-treated hemoglobin precursor, this sulfhemoglobin does not bind O2 cooperatively. Thus, sulfhemoglobin appears to be in a high affinity form at alkaline pH and a low affinity form at acid pH, similar to hemoglobin A. These results demonstrate that the magnitude of the Hill number is not always an indicator of the interaction between oxygen binding and other functions in a hemoglobin.

Carboxypeptidases↗
PubMed1992

1H nuclear magnetic resonance study of the prosthetic group in sulfhemoglobin.

The molecular and electronic structure of the modified prosthetic group of sulfhemoglobin (SHb) was investigated by 1H NMR for the low-spin ferric cyano-met and high-spin ferrous deoxy sulfhemoglobin complex. The 1H NMR resonances of the two subunits in the cyano-met SHb complex were differentiated on the basis of the differential stability toward regeneration of native subunits. The subunit origin for the two sets of resonances was established by formation of the sulfglobin protein for the isolated alpha-chain prior to assembling with the native beta-subunit to yield a tetramer with sulfhemin in the alpha-subunits. The subunit peak assignments establish that it is the beta-subunit of SHb which regenerates more rapidly to native protein. The hyperfine shifted sulfhemin peaks were assigned based on steady-state nuclear Overhauser effects which demonstrated that similarly hyperfine shifted peaks exhibit the same dipolar connectivities observed in the analogous sulfmyoglobin complex. Hence it is concluded that pyrrole B is the site of reaction in both hemoglobin and myoglobin. The initially formed SHb complex failed to equilibrate to yield a complex with a sulfhemin sufficiently stable to extraction as found previously for sulfmyoglobin. However, apoHb readily bound the green sulfhemin extracted from the terminal alkaline equilibration product of sulfmyoglobin. The inhibition on the equilibration to the alkaline form with the exocyclic thiolene ring is attributed to the interaction with Val FG5. The observations of the same dipolar connectivities among similarly hyperfine shifted peaks in the directly prepared and reconstituted SHb complexes further support the same structure for the sulfhemin in sulfmyoglobin and SHb. The strongly hyperfine shifted peaks in the deoxy form of both SHb complexes were found very similar to those of the analogous sulfmyoglobin complexes. The proximal His labile ring proton signal appears to experience a 5- to 10-ppm decrease upon conversion of a native globin to sulfglobin. This attenuation may provide a probe for differentiating chlorins and hemins in globin pockets.

Humans↗
PubMed1977

[Studies on sulfhemoglobin formation by various drugs (2) (author's transl)].

Sulfhemoglobin (SHb) and methemoglobin (MHb) formations by various aniline erivatives were examined by a single and three consecutive intraperitoneal administrations to mice. It was found that with a single administraion, methemoglobinemia was induced by aniline, 2-methylaniline, 3-methylaniline, 4-methylaniline, 3-trifluoromethylaniline (3-TFMA), 4-trifluoromethylaniline (4-TFMA), 2, 3-dichloroaniline, 2-aminopehnol, acetanilide (AA), 2-hydroxyacetanilide, N-methylaniline (NMA), N,N-dimethylaniline (NDMA), N-ethylaniline (NEA) and N,N-diethylaniline, and was not observed with 2, 3-dimethylanilnie, 2-trifluoromethylaniline, 3-aminophenol, 4-aminophenol, 2. 6-dichloroaniline, 3-hydroxyacetanilide (3-HAA), 4-hydroxyacetanilide (4-HAA), 2-aminobenzoic acid, 3-aminobenzoic acid, 4-aminobenzoic acid and 4-chloro-2-aminobenzoic acid. On the other hand, sulfhemoglobinemia which appeared much more delayed than MHb, with a single administration, was found to be induced by 3-TFMA, 4-TFMA and NMA. Furthermore, with three consecutive administrations, such was induced by AA, 3-HAA, NDMA and NEA even though SHb was not demonstrated with a single administration. Structure-SHb and MHb forming property relationships were discussed.

Aniline Compounds↗
PubMed1977

[Studies of sulfhemoglobin formation by various drugs (3) (author's transl)].

Sulfhemoglobin (SHb) and methemoglobin (MHb) formations by various compounds were examined by single and three consecutive intraperitoneal administrations to mice. With a single administration, methemoglobinemia was induced by diphenylamine (DPA), 1-naphthylamine (NA), phenylnaphthylamine (PNA), N-(1-naphthyl) anthranilic acid (N1) and N-(1'-naphthyl)-2-aminophenylacetic acid (IG240), and was not observed with phenylanthranilic acid (PAA), N-benzoyl-N'-phenyl-2, 6-diaminobenzoic acid (BPAA), flufenamic acid (FA), mefenamic acid (MFA), N-(2-6-dichlorophenyl) anthranilic acid (CPAA), N-(2', 6'-dichlorophenyl)-2-aminophenylacetic acid (CPPA), nine derivatives of N1 and two derivatives of IG240. On the other hand, sulfhemoglobinemia, with a single administration, was found to be induced by NA. Furthermore, with three consecutive administrations, such was induced by DPA, PAA, BPAA and FA even though SHb was not demonstrated with a single administration, and was not observed with MF, CPAA, CPPA and various derivatives of N1 and IG240.

1-Naphthylamine↗
PubMed1975

[Formation of sulfhemoglobin using various drugs].

It is well known that aniline and hydroxylamine derivatives induce methemoglobinemia in humans as well as various animal species. It was noticed that sulfhemoglobinemia was induced by subchronic administration of N-(4-chlorophenyl)-beta-(4-hydroxymethylphenoxy)ethylurethane (HPU) to rabbits (p.o.), cats (i.p.) and mice (i.p.). Sulfhemoglobin (SHb) and methemoglobin (MHb) formation by various compounds structurally related to HPU were examined by a single and three consecutive intraperitoneal administrations to mice. It was found that by a single administration, methemoglobinemia was induced by phenylhydroxylamine (PHA), nitrobenzene (NB), aniline (A), 2-chloro-A (2-Cl-A), 3-Cl-A, 4-Cl-A, acetanilide (AA), phenacetin (PA), N-(4-chlorophenyl)ethylurethane (CPU), hydroxylamine (HA) and sodium nitrite (SN), and was not observed with phenylurethane, HPU, methylhydroxylamine (MHA), methylamine and nitromethane (NM). On the other hand, with sulfhamoglobinemia which appeared much more delayed than MHb, a single administration, was found to be induced by PHA, 3-Cl-A, 4-Cl-A, PA, CPU, MHA and SN. Furthermore, with three consecutive administrations, such was induced by NB, 2-Cl-A, AA, HPU and NM even though SHb was not demonstrated with a single administration. Structure-SHb forming property relationship and mechanism for SHb formation are discussed.

Acetanilides↗
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↗
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↗
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↗
PubMed1979

Shunt effect of carboxyhemoglobin.

Estimation of intrapulmonary blood shunt fraction requires accurate evaluation of pulmonary capillary, arterial, and mixed venous oxygen contents. The presence of carboxyhemoglobin, as well as methemoglobin and sulfhemoglobin, may lead to large errors in the calculated intrapulmonary blood shunt fraction. The errors are most pronounced at low values of carboxyhemoglobin and low values of true intrapulmonary shunt fraction.

Carboxyhemoglobin↗
PubMedDate not supplied

[The chemical action of gun powder gases on biological tissues in a point-blank shot].

Chemical effect of gun powder gas on the biologic tissues manifests by red-brown staining of the tissues, mainly at the expense of methemoglobin and sulfhemoglobin. Scarlet staining of the tissues at the edges of gun-shot wounds is not a specific marker of a shot made from a short distance; it may emerge several hours after wounding at the expense of hydroxy-hemoglobin and is not at all related to the chemical effect of gun powder gas. The conditions conducive to scarlet staining are an open wound permitting free oxygenation by air oxygen and hemoglobin transfer from the injured red cells into blood plasma and adjacent tissues.

Animals↗
PubMed1979

[Preoperative care and accumulation of non-active hemoglobin derivatives in blood of patients].

A study of the concentration of met- and sulfhemoglobine in patients on admission to the clinic and at the end of the preoperative management and treatment was carried out upon 35 surgical cases. The medicamentous therapy included the drugs favouring the restoration of methemoglobin (10.20% and 40% glucose solutions, ascorbic acid etc.). Therewith the concentration of non-active hemoglobine derivatives dropped at the end of the preoperative management and treatment.

Acute Disease↗
PubMed1977

Sulfhaemoglobin. Absorption spectrum, millimolar extinction coefficient at lambda = 620 nm, and interference with the determination of haemoglobin and of haemiglobincy anide.

The spectrophotometry properties of sulfhaemoglobin (SHb) and some derivatives were investigated using an improved technique for measuring the SHb fraction induced in human blood samples. The millimolar extinction coefficient of SHb at lambda = 620 nm was found to be 20.8 (S.D. 1.48; S.E. = 0.44; n = 11). In addition it was demonstrated that the spectral changes occurring in SHb containing haemoglobin solutions upon the addition of KCN, K3Fe(CN)6 and K3Fe(CN)6 +KCN invalidate the KCN addition method for the determination of haemiglobin. The influence of clinically occurring SHb fractions on the internationally standarized total haemoglobin determination were shown to be insignificant.

Ferricyanides↗
PubMed1975

Demonstration of lag phase in the sol-gel transformation of deoxygenated S hemoglobin without temperature alteration.

1). During the sol to gel transformation of deoxygenated sickle hemoglobin, a time-dependent process preceding gel formation (lag phase) was demonstrated that was inversely proportional to a function of the hemoglobin concentration and that occurred without alteration in temperature, pH, or oxygen tension. 2). As determined by the Schachman modification of the capillary viscometer, preparations of oxyhemoglobin S and A and deoxyhemoglobin A were indistinguishable when compared over a wide range of concentrations. Up to the concentration at which gelling occurred, deoxyhemoglobin S exhibited the same viscosity behavior. The viscosity of deoxygenated hemoglobin S within the lower gelling concentration range was normal during the lag phase and became abnormally high only at the time of gelation.

Anemia, Sickle Cell↗
PubMed1975

Abnormal red cell metabolism in patients with chronic uremia: Nature of the defect and its persistence despite adequate hemodialysis.

A red cell metabolic abnormality, which diminishes the maximum activity of the pentose phosphate shunt, occurs in some uremic patients, even those adequately dialyzed with fluids prepared from distilled or charcoal-filtered water. Within individual patients the severity of this abnormality does not change even after 9 mo of consecutive hemodialyses. However, between patients it does correlate inversely with hematocrit. When erythrocytes from patients with the abnormality are stressed with oxidant compounds, such as ascorbate, erythrocyte glucose consumption and lactate formation are abnormally increased, while lactate/pyruvate ratios abnormally diminish. Concomitantly, red cell glycolytic intermediates, including fructose-1,6-diphosphate, glyceraldehyde-3-phosphate, 3-phosphoglycerate, phosphoenol pyruvate, and pyruvate, markedly accumulate. Surprisingly, no increase of 2-phosphoglycerate occurs, which suggests that inefficient phosphoglyceromutase activity underlies this perturbation of erythrocyte metabolism and its associated hemolytic process.

Ascorbic Acid↗
PubMed1979

Plasma inhibitors of the erythrocyte hexose monophosphate shunt in uraemia.

Sulphaemoglobin production, induced by an oxidative stress (ascorbate and cyanide) has been studied in uraemic patients. Results are expressed as the ratio of optic density of sulphaemoglobin (620nm) to optic density of total haemoglobin (540nm). The mean (+/- SEM) ratio found was 0.35 +/- 0.03 in 28 controls and 0.56 +/- 0,03 in 51 uraemic subjects (p less than 0.001). Cross incubation tests demonstrated that the anomaly was caused by a plasma factor. In vitro studies - guanidinic compounds added to control erythrocyte suspensions before incubation - suggest that this factor might be guanidinic propionic acid.

Anemia, Hypochromic↗