Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Hamilton, Howard B.; Iuchi, I; Miyaji, T; Shibata, Susumu

doi:10.1172/jci106010

Cited by 67 publications

(12 citation statements)

References 35 publications

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“…In recent years, studies of families with dominantly inherited erythrocytosis have established hemoglobinopathy as the main etiologic possibility (4-9). Thus far, in all the families with hemoglobinopathic erythrocytosis, an abnormal hemoglobin was readily demonstrable with electrophoretic or chromatographic techniques (4)(5)(6)(7)(8)(9). This, however, is not necessary for diagnosis.…”

Section: Discussionmentioning

confidence: 99%

“…The delineation of the structural and functional aberrations of these hemoglobins and the elucidation of the pathophysiological basis of crythrocytosis have contributed significantly to the understanding of molecular disease in man (1)(2)(3)(4). Abnormal electrophoretic or chromatograp)hic patterns are characteristic of all the described mutants (4)(5)(6)(7)(8)(9). We report a new variant associated with abnormal oxygen equilibria and erythrocytosis which was defined only after detailed structural studies on isolated globin chains.…”

Section: Introductionmentioning

confidence: 99%

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Hemoglobin Olympia (β20 Valine → Methionine): An Electrophoretically Silent Variant Associated with High Oxygen Affinity and Erythrocytosis

Stamatoyannopoulos¹,

Nute²,

Adamson³

et al. 1973

J. Clin. Invest.

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A B s T R A C T In a family with erythrocytosis, electrophoretic and chromatographic studies failed to demonstrate a hemoglobin variant. However, the oxygen dissociation curves of affected individuals were shifted to the left of normal and this shift persisted when oxygen equilibria were studied in 2,3-diphosphoglycerate-stripped hemolysates. A mutant hemoglobin was evidently present in the red blood cells of the affected persons and was responsible for the increased oxygen affinity and erythrocytosis. Specific staining of tryptic peptidle maps of P-chains from the propositus showed that peptide PT3 was positive for a sulfur-containing amino acid. Amino acid analysis yielded a composition identical to that of normal PT3, except that there were 2.6 residues of valine and 0.4 residues of methionine (normal composition: Val = 3.0, Met = 0). This suggested that the P-chains of affected individuals consisted of a mixture of two kinds of chains, 40% of which had a methionyl residue in PT3. Structural studies of isolated cyanogen bromide fragments demonstrated unequivocally that, in the abnormal P-chains, valine in position 20 is replaced by methionine. The new hemoglobin mutant is designated hemoglobin Olympia (P20 (B2) valine >methion-ine).

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Hemoglobin Olympia (β20 Valine → Methionine): An Electrophoretically Silent Variant Associated with High Oxygen Affinity and Erythrocytosis

Stamatoyannopoulos¹,

Nute²,

Adamson³

et al. 1973

J. Clin. Invest.

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“…At least 10 different variants have been reported (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). With the exception of Hb Olympia (12), these abnormal hemoglobins can be separated from Hb A by electrophoresis or chromatography.…”

Section: Introductionmentioning

confidence: 99%

Hemoglobin Brigham (α2Aβ2100 Pro→Leu). HEMOGLOBIN VARIANT ASSOCIATED WITH FAMILIAL ERYTHROCYTOSIS

Lokich¹,

Moloney²,

Bunn³

et al. 1973

J. Clin. Invest.

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“…This interaction is disrupted in several high O 2 affinity variants with b146 substitutions: Hb Hiroshima (b146 [HC3] His . Asp) (Hamilton et al 1969;Perutz et al 1971;Imai et al 1972;Olson et al 1972), Hb York (b146 [HC3] His . Pro) (Bare et al 1976), and Hb Cowtown (b146 [HC3] His .…”

Section: High Oxygen Affinity Variantsmentioning

confidence: 99%

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Thom

Dickson

Gell

et al. 2013

Cold Spring Harbor Perspectives in Medicine

225

182

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Diseases affecting hemoglobin synthesis and function are extremely common worldwide. More than 1000 naturally occurring human hemoglobin variants with single amino acid substitutions throughout the molecule have been discovered, mainly through their clinical and/or laboratory manifestations. These variants alter hemoglobin structure and biochemical properties with physiological effects ranging from insignificant to severe. Studies of these mutations in patients and in the laboratory have produced a wealth of information on hemoglobin biochemistry and biology with significant implications for hematology practice. More generally, landmark studies of hemoglobin performed over the past 60 years have established important paradigms for the disciplines of structural biology, genetics, biochemistry, and medicine. Here we review the major classes of hemoglobin variants, emphasizing general concepts and illustrative examples.

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Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Cited by 67 publications

References 35 publications

Hemoglobin Olympia (β20 Valine → Methionine): An Electrophoretically Silent Variant Associated with High Oxygen Affinity and Erythrocytosis

Hemoglobin Olympia (β20 Valine → Methionine): An Electrophoretically Silent Variant Associated with High Oxygen Affinity and Erythrocytosis

Hemoglobin Brigham (α2Aβ2100 Pro→Leu). HEMOGLOBIN VARIANT ASSOCIATED WITH FAMILIAL ERYTHROCYTOSIS

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

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