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)
Pages (from-to)759-762,IN51-IN52,763-766
JournalJournal of Molecular Biology
Volume89
Issue number4
DOIs
StatePublished - Nov 15 1974

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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