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Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism
Journal article   Open access   Peer reviewed

Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism

F A Ferrone, J Hofrichter, H R Sunshine, W A Eaton and National Institutes of Health, Bethesda, MD
Biophysical journal, v 32(1), pp 361-380
01 Oct 1980
PMID: 7248455
url
https://doi.org/10.1016/s0006-3495(80)84962-9View
Published, Version of Record (VoR)Open Access (Publisher-Specific) Open
url
https://doi.org/10.1016/S0006-3495(80)84962-9View
Published, Version of Record (VoR) Open

Abstract

The kinetics of deoxyhemoglobin S gelation have been investigated using photolytic dissociation of the carbon monoxide complex to initiate the process. Measurements over a wide range of times, 10(-3)-10(4) show that both the concentration dependence of the tenth-time (i.e., the time required to complete one-tenth the reaction) and the time dependence of the process decrease as gelation speeds up. In slowly gelling samples, where single domains of polymers are formed in the small sample volumes employed with this technique (1-2 x 10(-9) cm3), there is a marked increase in the variability of the tenth-times. These results are explained by a mechanism in which gelation is initiated by homogeneous nucleation of polymers in the bulk solution phase, followed by heterogeneous nucleation on the surface of existing polymers. At the lowest concentrations, homogeneous nucleation is so improbable that stochastic behavior is observed in the small sample volumes, and heterogeneous nucleation is the dominant pathway for polymer formation, thereby accounting for the high time dependence. At the highest concentrations homogeneous nucleation becomes much more probable, and the time dependence decreases. The decrease in concentration dependence of the tenth-time with increasing concentration results from a decrease in size of both the homogeneous and heterogeneous critical nuclei. The model rationalizes the major observations on the kinetics of gelation of deoxyhemoglobin S, and is readily testable by further experiments.

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