Length distributions of hemoglobin S fibers

Robin W. Briehl, Eric S. Mann, Robert Josephs

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Electron microscopy of sickle cell hemoglobin fibers fixed at different times during gelation shows an exponential distribution of fiber lengths, with many short fibers and few long ones. The distribution does not change significantly with time as polymerization progresses. If this distribution of lengths reflects kinetic mechanism of fiber assembly, it complements information from studies of the progress of average properties of the polymers and, as has been done for other rod-like polymerizing systems, permits testing of models for the mechanism of fiber assembly. In this case, the results are consistent with the double nucleation model of Ferrone et al. or with a related alternative model based on fiber breakage. However, other possible causes of this microheterogeneity exist, including: breakage due to solution shearing of the long, rod-like, fibers; the presence of residual nuclei; equilibrium relations governing polymerization; and breakage of solid-like but weak gels that develop early and adhere to the grid. The arguments against the first three of these possibilities suggest that they are not responsible. However, breakage of entanglements or cross-links in a solid-like and adherent gel is consistent with the distributions.

Original languageEnglish (US)
Pages (from-to)693-698
Number of pages6
JournalJournal of Molecular Biology
Volume211
Issue number4
DOIs
StatePublished - Feb 20 1990

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Sickle Hemoglobin
Polymerization
Gels
Electron Microscopy
Polymers

ASJC Scopus subject areas

  • Virology

Cite this

Length distributions of hemoglobin S fibers. / Briehl, Robin W.; Mann, Eric S.; Josephs, Robert.

In: Journal of Molecular Biology, Vol. 211, No. 4, 20.02.1990, p. 693-698.

Research output: Contribution to journalArticle

Briehl, Robin W. ; Mann, Eric S. ; Josephs, Robert. / Length distributions of hemoglobin S fibers. In: Journal of Molecular Biology. 1990 ; Vol. 211, No. 4. pp. 693-698.
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