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Monomer diffusion into polymer domains in sickle hemoglobin
Journal article   Open access   Peer reviewed

Monomer diffusion into polymer domains in sickle hemoglobin

M R Cho and F A Ferrone
Biophysical journal, v 58(4), pp 1067-1073
Oct 1990
PMID: 2248990
url
https://doi.org/10.1016/S0006-3495(90)82449-8View
Published, Version of Record (VoR) Open

Abstract

Hemoglobin, Sickle - chemistry Biophysical Phenomena Humans Biophysics Thermodynamics Hemoglobins - chemistry Photolysis Light Scattering, Radiation Gels - chemistry Diffusion In Vitro Techniques Spectrophotometry
The gelation of sickle hemoglobin includes the formation of spherulitic arrays of polymers, known as polymer domains, which are an intrinsic result of the polymer formation mechanism. We have observed the diffusion of monomers into domains as they form, which substantially increases the total concentration of hemoglobin within the domain. The maximum total concentration attained is comparable with the pellet concentration of 0.5-0.55 g/cm3 obtained in sedimentation experiments. The half time for this process is approximately 50 s for domains of 25 microns radius, and is approximately independent of temperature. The shape of the diffusion progress curves as well as the deduced diffusion constants, and their weak temperature dependence are consistent with a simple model of hemoglobin monomer diffusion into the domain.

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Biophysics
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