Structure of Haemoglobin M Milwaukee, A Mutant Form Exhibiting Interaction Between Ferrous and Ferric Subunits
- 147 Downloads
There are five different abnormal haemoglobins which cause methaemoglobinaemia. In four of these the action of methaemoglobin reductase is ineffective because either the proximal or the distal haem-linked histidines in one pair of subunits have been replaced by tyrosines, and in the fifth, known as haemoglobin M Milwaukee (Hb Mil), because valines Ell(67) β have been replaced by glutamic acids (Gerald and Efron, 1961).
KeywordsIron Atom Difference Spectrum Oxygen Affinity Ferrous Citrate Porphyrin Ring
Unable to display preview. Download preview PDF.
- Hoard, J.L. (1968). In: Structural Chemistry and Molecular Biology (edit, by Rich, A., and Davidson, N.) Freeman: San Francisco.Google Scholar
- Lindstrom, T.R., Ho, C., and Pisciotta, A.V. (1972). Nuclear magnetic resonance studies of haemoglobin M Milwaukee-1 and their implications to haem-haem interactions. Nature. In press.Google Scholar
- Perutz, M.F. (1972). The nature of haem-haem interaction. Nature. In press.Google Scholar