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A hypothesis for the increased oxygen affinity in haemoglobin Malmö
British Journal of Haematology
|May 1, 1976
Summary
Hemoglobin Malmö, a variant with high oxygen affinity causing erythrocytosis, is inherited dominantly. A novel chemical bond explains its high oxygen affinity and related physiological effects.
Area of Science:
- Biochemistry
- Hematology
- Molecular Biology
Background:
- Hemoglobin Malmö (beta97His to Gln) is an autosomal dominant high oxygen affinity hemoglobin.
- This variant is associated with secondary erythrocytosis.
Purpose of the Study:
- To present a hypothesis explaining the high oxygen affinity, hyperbolic dissociation curve, and Bohr effect of Hemoglobin Malmö.
- To provide biochemical and functional data supporting this hypothesis.
Main Methods:
- Purification of abnormal hemoglobin from a family with Hemoglobin Malmö.
- Biochemical and functional analysis of the purified hemoglobin.
- Application of Perutz's allosteric model.
Main Results:
- Experimental data support a hypothesis for Hemoglobin Malmö's properties.
- A specific chemical bond formation is proposed as the mechanism for high oxygen affinity.
- This bond involves the beta93 cysteine and the substituted beta97 glutamine.
Conclusions:
- The high oxygen affinity of Hemoglobin Malmö is explained by a novel chemical bond.
- This finding provides insight into hemoglobinopathies and oxygen transport.
- The study supports the allosteric model in explaining hemoglobin function.