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Literature DB >> 4515930

Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas.

Abstract

The isolated beta subunit of hemoglobin Kansas has an oxygen affinity that is as low relative to the oxygen affinity of the beta(A) subunit as the affinity of hemoglobin Kansas is low relative to hemoglobin A. Thus the low affinity properties of hemoglobin Kansas are almost completely reflected in the properties of the isolated subunits. The kinetic results show that the equilibrium affinity difference results both from a much larger oxygen dissocation rate constant in beta(Kansas) (k = 37 sec(-1) and 18 sec(-1) for beta(Kansas) and beta(A), respectively) and from a lower association reaction rate, The properties of the alpha chains from hemoglobins A and Kansas appear to be identical, as expected.

Entities: Chemical Gene

Mesh：

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Year: 1973 PMID： 4515930 PMCID： PMC433580 DOI： 10.1073/pnas.70.6.1718

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

13 in total

1. States of hemoglobin in solution.

Authors: R T Ogata; H M McConnell
Journal: Biochemistry Date: 1972-12-05 Impact factor: 3.162

2. The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin.

Authors: J S Olson; Q H Gibson
Journal: J Biol Chem Date: 1972-03-25 Impact factor: 5.157

3. Equilibria and kinetics of ligand binding by leghemoglobin from soybean root nodules.

Authors: T Imamura; A Riggs
Journal: J Biol Chem Date: 1972-01-25 Impact factor: 5.157

4. Molecular pathology of human haemoglobin.

Authors: M F Perutz; H Lehmann
Journal: Nature Date: 1968-08-31 Impact factor: 49.962

5. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium.

Authors: J Bonaventura; A Riggs
Journal: J Biol Chem Date: 1968-03-10 Impact factor: 5.157

6. Dissociation of haemoglobin Chesapeake into subunits.

Authors: H F Bunn
Journal: Nature Date: 1970-08-22 Impact factor: 49.962

7. Stereochemistry of cooperative effects in haemoglobin.

Authors: M F Perutz
Journal: Nature Date: 1970-11-21 Impact factor: 49.962

8. Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant.

Authors: S Tomita; A Riggs
Journal: J Biol Chem Date: 1971-02-10 Impact factor: 5.157

Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas.

1. States of hemoglobin in solution.

2. The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin.

3. Equilibria and kinetics of ligand binding by leghemoglobin from soybean root nodules.

4. Molecular pathology of human haemoglobin.

5. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium.

6. Dissociation of haemoglobin Chesapeake into subunits.

7. Stereochemistry of cooperative effects in haemoglobin.

8. Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant.

9. Preparation and properties of alpha- and beta-chains from human hemoglobin.

10. The binding of carbon monoxide to and chains in tetrameric mammalian hemoglobin.

Review 1. Hemoglobin variants: biochemical properties and clinical correlates.

2. An alternative theoretical formula for hemoglobin oxygenation.

3. The Second and Third Hemoglobin Kansas Cases in the Turkish Population.