1974
DOI: 10.1016/0014-5793(74)80975-0
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Hemoglobin E: Its oxygen affinity in relation with the ionic environment

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Cited by 6 publications
(8 citation statements)
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References 12 publications
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“…Ligand binding properties and allosteric parameters all indicate very minor differences in CO or O 2 reactivity between HbE and HbA. Based on the structural comparisons and the CO recombination measurements, it is not surprising that the oxygen affinity is not significantly affected by the mutation according to earlier reports (19,20) and confirmed by our results.…”
Section: Discussionsupporting
confidence: 76%
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“…Ligand binding properties and allosteric parameters all indicate very minor differences in CO or O 2 reactivity between HbE and HbA. Based on the structural comparisons and the CO recombination measurements, it is not surprising that the oxygen affinity is not significantly affected by the mutation according to earlier reports (19,20) and confirmed by our results.…”
Section: Discussionsupporting
confidence: 76%
“…Oxygen Binding Properties-A limited series of oxygen affinity measurements conducted at high and low salt concentrations in phosphate buffer, pH 7.4, revealed the same minor differences in the P 50 and Hill coefficient between HbA and HbE as reported previously (19,20). Overall, the results are consistent with earlier reports that HbE oxygen binding is similar to HbA (19).…”
Section: Functional Studiessupporting
confidence: 82%
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“…The 0,-dissociation curve, right-shfted when she was anemic, became nearly normal (but still perceptibly right-shfted) after treatment to correct concurrent iron-deficiency anemia, when the venous hemoglobin concentration was 12 gm/dl and 2,3-diphosphoglycerate concentration was also normal. Gacon et a1 [38] also studied the 0, affinity of hemoglobin E in a nonanemic (presumed) homozygote and found, when using intact erythrocytes, a distinctly right-shifted dissociation curve (p50 was 36 mm Hg), together with increased erythrocytic 2,3-diphosphoglycerate. Paradoxically, Gacon and co-workers also reported a distinct increase in O 2 affinity when purified hemoglobin E was examined in a low salt concentration.…”
Section: Discussionmentioning
confidence: 94%
“…We had recently the opportunity of studying hemoglobin E in various kinds of association (heterozygous A, E and E-/3" thalassemia) and in homozygous E, and demonstrated that the structural abnormality, located in a contact area between subunits, gave rise to some discrete functional disorders [3].…”
mentioning
confidence: 99%