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Ultrastructural Features of Erythrocyte and Hemoglobin Sickling
James G. White, MD
Arch Intern Med. 1974;133(4):545-562.
Abstract
Hemoglobin polymerization develops from a process of condensation, molecular interaction, aggregation, and assembly. Molecular organization of structures formed during polymerization depends on the type of hemoglobin, its specific defect, and its state of oxygenation. Sickling exemplifies hemoglobin polymerization. In the reduced state, sickle hemoglobin (HbS), alone or in combination with other hemoglobins, undergoes condensation, aggregation, and assembly into long rod-like structures. Oxygenated or reduced normal and abnormal hemoglobins and oxy-HbS also polymerize; they form aggregates, microtubules, or crystals rather than rods. Crystals form from aggregates, microtubules or rods, but molecular reorganization of the earlier structures into a new lattice is required. Thus, sickling is due to sol-gel transformation rather than crystallization, and polymers of HbS are unique because they differ in molecular organization from hemoglobin aggregates, microtubules, and crystals.
Author Affiliations
Minneapolis
From the Department of Pediatrics, University of Minnesota Medical Center, Minneapolis.
Footnotes
Received for publication June 12, 1973; accepted June 15.
Reprint requests to Box 248 Mayo Memorial Bldg, Minneapolis, MN 55455 (Dr. White).
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