Hemoglobin Hirosaki (α 43 [CE 1] Phe→Leu), a new unstable variant

Ohba, Yusuke; Miyaji, T; Matsuoka, M; Yokoyama, Masaru; Numakura, Hirohiko; Nagata, Kishiro; Takebe, Y; Izumi, Yukio; Shibata, Susumu

doi:10.1016/0005-2795(75)90325-6

Cited by 32 publications

(1 citation statement)

References 17 publications

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“…Hb Hirosaki (a2 43 [CE1] Phe . Leu) was discovered in a family with hemolytic anemia (Ohba et al 1975;Tanaka et al 2005). After several tests failed to identify a soluble variant Hb within erythrocytes, DNA sequencing was used to characterize the mutation.…”

Section: Selected Variants That Illustrate Important Aspects Of Hemogmentioning

confidence: 99%

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Thom

Dickson

Gell

et al. 2013

Cold Spring Harbor Perspectives in Medicine

218

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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Section: Selected Variants That Illustrate Important Aspects Of Hemogmentioning

confidence: 99%

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Thom

Dickson

Gell

et al. 2013

Cold Spring Harbor Perspectives in Medicine

218

182

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A new Spanish family with Hb Louisville

et al. 1989

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The clinical, hematological, and biochemical characteristics of a new family with heterozygous hemoglobin (Hb) Louisville are described. The family showed a decrease in both oxygen affinity and cooperativity with the normal Bohr effect. This family has the greatest number of affected members reported to date. Among the descendants, two first cousins (III-10 and III-11), both of whom are affected by the heterozygous trait of Hb Louisville, had had three abortions of undetermined causes.

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Unstable and Thalassemic α Chain Hemoglobin Variants: A Cause of Hb H Disease and Thalassemia Intermedia

et al. 2008

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We report an update of the alpha-globin gene point mutations resulting in structural modification associated with an alpha-thalassemia (alpha-thal) phenotype. These variants, barely symptomatic in the heterozygous state, are either unstable due to folding defects and/or defects in binding to alpha-hemoglobin stabilizing protein (AHSP). This is predicted to result in precipitation of the unstable alpha chains or Hb variant, a concomitant decrease in the overall quantity of normal alpha-globin in the red cells and a potential degree of anemia and possibly, hemolysis. Genotype/phenotype correlation and potential genetic risk in combination with common or less common alpha-thal defects are discussed.

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Hemoglobin Hirosaki (α 43 [CE 1] Phe→Leu), a new unstable variant

Cited by 32 publications

References 17 publications

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

A new Spanish family with Hb Louisville

Unstable and Thalassemic α Chain Hemoglobin Variants: A Cause of Hb H Disease and Thalassemia Intermedia

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