Gelation of sickle cell haemoglobin. II. Methaemoglobin

Robin W. Briehl, Sandra M. Ewert

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Abstract

Sickle cell methaemoglobin was assayed for gel formation by an equilibrium ultracentrifugation method previously described. A phase change from sol to gel, indicative of gelation, occurred, depending on conditions, at concentrations between 0.35 and 0.5 g/ml, considerably higher than concentrations observed previously for gelation of deoxyhaemoglobin S. Inositol hexaphosphate favours gelation, but gelation is seen also in its absence. Lowering pH toward 6 favours gelation. If gelation is assumed to require molecules in the T quaternary conformation, these results provide further evidence that methaemoglobin exists in R-T equilibrium in solution and that this equilibrium lies between the extremes exhibited by deoxyhaemoglobin (T-state) and carbon monoxide or oxyhaemoglobin (R-state).

Original languageEnglish (US)
JournalJournal of Molecular Biology
Volume89
Issue number4
DOIs
StatePublished - Nov 15 1974

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Sickle Hemoglobin
Methemoglobin
Gels
Oxyhemoglobins
Phytic Acid
Ultracentrifugation
Polymethyl Methacrylate
Carbon Monoxide
deoxyhemoglobin
sickle methemoglobin

ASJC Scopus subject areas

  • Virology

Cite this

Gelation of sickle cell haemoglobin. II. Methaemoglobin. / Briehl, Robin W.; Ewert, Sandra M.

In: Journal of Molecular Biology, Vol. 89, No. 4, 15.11.1974.

Research output: Contribution to journalArticle

Briehl, Robin W. ; Ewert, Sandra M. / Gelation of sickle cell haemoglobin. II. Methaemoglobin. In: Journal of Molecular Biology. 1974 ; Vol. 89, No. 4.
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