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Evidence for Improved Fitness

Griffin P. Rodgers, MD

Arch Intern Med. 1988;148(5):1019-1020.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

Sickle cell anemia is the first disease to be understood on a molecular level.¹ The amino acid valine replaces the normal glutamic acid residue at the sixth position of the β-globin chain, the consequence of a GAG to GTG codon mutation. The resultant sickle hemoglobin, or HbS (₂β^s₂) has a peculiar tendency to self-associate and form long strands of polymer on deoxygenation, which leads to red cell morphologic changes and to abnormal rheologic properties in the microcirculation.²

See also p 1140.

The primary determinants of the rate and extent of hemoglobin S polymerization, at any given oxygen saturation, are the intracellular hemoglobin concentration and hemoglobin composition (fraction of S and non-S hemoglobins). In addition, the ambient temperature, 2,3-diphosphoglycerate concentration, and pH can affect the polymerization tendency, albeit to a lesser extent, under normal physiologic conditions.^2,3 Thus, the hemolytic and overall clinical severity of . . . [Full Text PDF of this Article]

Author Affiliations
Laboratory of Chemical Biology National Institute of Diabetes and Diseases of the Kidney National Institutes of Health Bldg 10, Room 9N-314 Bethesda, MD 20892

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