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The polymerization of sickle hemoglobin in solutions and cells
Journal article   Peer reviewed

The polymerization of sickle hemoglobin in solutions and cells

F A Ferrone
Experientia, v 49(2)
15 Feb 1993
PMID: 8440349

Abstract

Erythrocytes, Abnormal - chemistry Thermodynamics Hemoglobin, Sickle - chemistry Solutions Humans Oxyhemoglobins - chemistry Erythrocytes, Abnormal - ultrastructure Anemia, Sickle Cell - blood Erythrocytes - chemistry Kinetics In Vitro Techniques Polymers
The polymerization of sickle hemoglobin occurs by the same mechanisms in solutions and in cells, and involves the formation of 14 stranded fibers from hemoglobin molecules which have assumed a deoxy quaternary structure. The fibers form via two types of highly concentration-dependent nucleation processes: homogeneous nucleation in solutions with hemoglobin activity above a critical activity, and heterogeneous nucleation in similarly supersaturated solutions which also contain hemoglobin polymers. The latter pathway is dominant, and creates polymer arrays called domains. The individual polymers bend, but also cross-link, and the resulting mass behaves as a solid. The concentration of polymerized hemoglobin increases exponentially unless clamped by rate limiting effects such as oxygen delivery.

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Web of Science research areas
Biochemistry & Molecular Biology
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