High Oxygen Affinity Hemoglobin Research Articles

Comparison of Hemoglobins Wood (α2β297 leu) and Malmö (α2β297 gln): Diagnostic Value of Citrate Agar Electrophoresis

Diagnostic value of citrate agar electrophoresis. Am J Clin Pathol 71:668-671, 1979. Of approximately three dozen hemoglobin variants that have greater than usual oxygen affinity, nearly half are inseparable from hemoglobin A by electrophoresis at pH 8.6. A comparison of hemoglobins Wood (alpha2beta297leu) and Malmö (alpha2beta297gln) is of interest from several standpoints. They represent similar substitutions at the identical locus in the beta chain. They result in identical clinical and hematologic manifestations. Oxygen affinities of these variants are identical. Both are poorly resolved from hemoglobin A by electrophoresis at pH 8.6. The position of each is identical when studied by isoelectric focusing in polyacrylamide gel. Finally, they are easily distinguished by citrate agar electrophoresis at pH 6.2. The excellent resolution of hemoglobins Malmö and Wood from each other results neither from difference in charge, nor size, nor in quaternary structure. This technic provides a simple but effective means for identifying and differentiating these hemoglobin variants. Comparison with the results of citrate agar electrophoresis of other high oxygen-affinity hemoglobins indicates that the findings for hemoglobins Malmö and Wood are unique and unambiguous.

Familial Relative Polycythaemia due to Haemoglobin Heathrow

Eleven affected members of a New Zealand family carrying the high oxygen affinity haemoglobin Heathrow are described. The detection of high oxygen affinity abnormal haemoglobins may be difficult as haemoglobin and red cell mass may both fall within the normal range and no abnormality may be detected on haemoglobin electrophoresis or by haemoglobin stability tests. The importance of oxygen affinity studies to establish the diagnosis is emphasized.

Familial relative polycythaemia due to haemoglobin heathrow

Eleven members of a New Zealand kindred who carried the high oxygen affinity Haemoglobin Heathrow are described. The difficulty of detection of high oxygen affinity haemoglobins are pointed out as haemoglobin and red cell mass fall within the normal range, and haemoglobin electrophoresis and haemoglobin stability tests may be normal. In such circumstances oxygen affinity studies are crucial for the diagnosis.

Hypoxic ventilatory response in subjects with normal and high oxygen affinity hemoglobins.

It has still not been shown unequivocally whether a decrement of arterial oxygen content or tension governs the ventilatory response to hypoxia. In an attempt to discriminate between the two possibilities, we have measured the ventilatory response to isocapnic progressive hypoxia in two healthy children with a high oxygen affinity hemoglobin (Hb Andrew-Minneapolis) and in their age- and sex-matched normal siblings. Hypoxic ventilatory response was identical in all subjects, there being no difference in minute ventilation at PAo2 = 40 mm Hg or in k (decrement of PO2 required to increase ventilation by a factor of 2.718). In contrast, at PAo2 = 40 mm Hg, hemoglobin oxygen saturation decreased markedly in controls but only slightly in high affinity subjects. Furthermore the increase in heart rate at PAo2 = 40 mm Hg was significantly less in high affinity subjects, suggesting a concomitant difference in oxygen delivery. Thus, with identical decrements in PAo2 but widely divergent changes in arterial oxygen content and oxygen delivery, controls and high affinity subjects showed virtually identical ventilatory response to hypoxia. We conclude that decrements of oxygen tension are the major stimulus for hypoxic ventilatory response.

Isolation of High Oxygen Affinity Hfmoclobins

This paper describes a method for isolating high oxygen affinity hemoglobins. It involves the selective derivatisation of the cysteine residue at position 93 in the beta chain. The iodoacetamide derivative of the high oxygen affinity hemoglobin was separated from the more negatively charged iodoacetic acid derivative of HbA on DEAE-Sephadex. The method was used to isolate two high oxygen affinity hemoglobins, one of which was subsequently identified as Hb Heathrow.

A hypothesis for the increased oxygen affinity in haemoglobin Malmö.

Haemoglobin Malmöbeta97His leads to Gln, a high oxygen affinity haemoglobin which causes secondary erythrocytosis, is transmitted in an autosomal dominant manner. A hypothesis accounting for the high oxygen affinity, hyperbolic oxyhaemoglobin dissociation curve, and the relatively normal Bohr effect is presented. The purified abnormal haemoglobin from the present family provided biochemical and functional data for this hypothesis based on the allosteric model proposed by Perutz. Experimental results support the formation of a chemical bond between the -SH proton of the beta93 cysteine and the amide of oxygen of the substituted beta97 glutamine as an explanation for the high oxygen affinity of haemoglobin Malmö.

Hemoglobin wood β97(FG4) His → Leu : A new high-oxygen-affinity hemoglobin associated with familial erythrocytosis

The characterization of hemoglobin Wood ( β97(FG4) His → Leu), a high oxygen affinity hemoglobin with reduced Hill constant is described. The amino acid substitution occurs at the α 1 β 2 interface, in the same position as in hemoglobin Malmö ( β97(FG4) His → Gln) and in an homologous position when compared with hemoglobins Chesapeake ( α92(FG4) Arg → Leu) and J. Capetown ( α92(FG4) Arg → Gln).

Structural and functional study of Hb Nancy β 145 (HC 2) Tyr → Asp a high oxygen affinity hemoglobin

FEBS LettersVolume 56, Issue 1 p. 39-42 Full-length articleFree Access Structural and functional study of Hb Nancy β 145 (HC 2) Tyr → Asp a high oxygen affinity hemoglobin Gérard Gacon, Gérard Gacon Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorHenri Wajcman, Henri Wajcman Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorDominique Labie, Dominique Labie Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorClaude Vigneron, Claude Vigneron Centre de Transfusion Sanguine, 54000 Nancy, FranceSearch for more papers by this author Gérard Gacon, Gérard Gacon Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorHenri Wajcman, Henri Wajcman Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorDominique Labie, Dominique Labie Institut de Pathologie Moléculaire 1 24, rue du faubourg Saint-Jacques, 75014 Paris, FranceSearch for more papers by this authorClaude Vigneron, Claude Vigneron Centre de Transfusion Sanguine, 54000 Nancy, FranceSearch for more papers by this author First published: August 01, 1975 https://doi.org/10.1016/0014-5793(75)80106-2Citations: 26 Groupe U 15 de l'Institut National de la Santé et de la Recherche Médicale, Laboratoire Associé au Centre National de la Recherche Scientifique. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume56, Issue1August 01, 1975Pages 39-42 ReferencesRelatedInformation

Nitrosylhemoglobin wood. Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum

Properties of Hb Wood (beta-97(FG4)His leads to Leu), a high oxygen affinity hemoglobin with reduced hemeheme interaction, were examined in its nitric oxide liganded form. The reactivity of the beta-93 thiol groups and the electron paramagnetic resonance (EPR) spectrum were examined to determine what effect the amino acid substitution, which occurs at the alpha1beta2 interface, would have on inositol hexaphosphate induced transition of this form of the tetramer. Binding of inositol hexaphosphate (IHP) in a 1:1 stoichiometry was demonstrated. In spite of apparently normal interaction with IHP, there was little or no change in the reactivity of the beta-93 thiol groups and in the electron paramagnetic resonance (EPR) spectrum as contrasted with the marked changes characteristic of normal hemoglobin (HbA). In contrast with NO-HbA, there was also no development of the EPR hyperfine structure in NO-Hb Wood with increased protonation of the protein at pH below 7.0. Taken together with the observations of Henry and Banerjee ((1973), J. Mol. Biol. 73, 469) on the development of NO-Hb EPR hyperfine structure and of Perutz et al. (1974a), Biochemistry 13, 2174) on changes in thiol reactivity with the R leads to T transition, the results suggest that IHP or H+ cannot switch NO-Hb Wood to the T conformation. Since the atomic structures of met- and deoxyhemoglobin offer no indication that His-97 plays any special part in the allosteric mechanism (M. E. Perutz, personal communication), it appears that the replacement of His-97 by Leu reduces the stability of the T structure relative to that of R.

Anemia in domestic cats: effect on hemoglobin components and whole blood oxygenation.

Phenylhydrazine-induced anemia in the domestic cat results in an increase in minor, high oxygen affinity hemoglobin B components and an accompanying decrease in the major, low affinity B component. This change is accompanied by an unusually large increase in erythrocytic adenosine triphosphate and 2,3-diphosphoglycerate, a slight decrease in the oxygen affinity of whole blood, and a large decrease in the Hill constant.

Effects of hyperoxia on survival of benthic marine invertebrates

1. 1. The effects of oxygen levels considerably in excess of air saturation on the survival of fourteen species of marine invertebrates were tested. 2. 2. The anemones Diadumene leucolena and Haliplanella luciae and the clam Mya arenaria suffered high mortality. 3. 3. Members of other species, including three hemoprotein-containing annelids, were not killed by prolonged exposure to hyperoxia. These results do not support the hypothesis that high oxygen affinity hemoglobins serve to buffer the tissues from otherwise toxic hyperoxia.

Responses of Aquatic Invertebrates to Declining Oxygen Conditions

Several models for the analysis of data relating the rate of oxygen uptake to environmental oxygen level have been evaluated. We conclude that the quadratic (or second-degree) polynomial, though hardly perfect, is the best. Data from 31 species of aquatic invertebrates are described by constants of the quadratic (or second-degree) polynomial equation. The results suggest a phylogenetic trend of increasing regulation of aerobic metabolism in response to declining environmental levels as animals acquire structures that effectively insulate their respiring tissue from the habitat. Many of these species apparently cease withdrawing oxygen from their external environment long before they have exhausted its supply. Presumably, those species with long lasting internal oxygen reservoirs, such as gas bubbles or pools of high oxygen affinity hemoglobin, continue to operate aerobic pathways, but those without substantial oxygen storage devices must switch over to anaerobic pathways, despite the availability of small residual volumes of external oxygen.

Maximum aerobic capacity and running performance at altitude.

Maximum aerobic capacity and running performance at altitude.

Polymorphism of turle hemoglobin and geographical differences int he frequency of variants of Chrysdemyspicta “slow” hemoglobin —an example of “temperature anti-adaptation”?

1. 1. The hemoglobin of all turtles of the specieis Pseudemys elegans and Chrysemys picat can be separated electrophoretically into “slow” and “fast” hemoglobin components. 2. 2. The “fingerprints” of tryptic digests of “fast” and “slow” hemoglobins differ by apptroximately one-third of the peptides. 3. 3. In C. picta there is individual variation int he electrophoretic properties of “slow”, but not “fast”, hemoglobin; nearly all C. picta have one of three “slow” hemoglobin phenotypes: S, D and S-D. 4. 4. The S variants is most common in C. picta from Minnesota and Wisconsins, whereas the D variants is most common in C. picta from Arkansas and Louisiana. 5. 5. The S variant has a much higher oxygen affinity than the D variant, regardless of the conditions under which the hemoglobin is studied. This is the opposite of what would be expected ont he basis of the prevalent “reasoning” in comparative physiology and temperature adaptation. 6. 6. A possible explanation forthe higher frequency of the high oxygen affinity hemoglobin in C. picta from the colder states is based on an extreme condition, such as lenght of time under ice, rather than an average condition, such as mean temperature.