Hemoglobin Cowtown (β146 HC3 His-Leu): A Mutant with High Oxygen Affinity and Erythrocytosis
Open Access
- 1 December 1979
- journal article
- case report
- Published by Oxford University Press (OUP) in American Journal of Clinical Pathology
- Vol. 72 (6) , 1028-1032
- https://doi.org/10.1093/ajcp/72.6.1028
Abstract
A new mutant, hemoglobin Cowtown, has been found in a white man and his father, both of whom have erythrocytosis. The father had previously been treated with 32P for polycythemia vera. The abnormal hemoglobin is not detectable on electrophoresis in alkaline buffers, but it resolves distinctively on electrophoresis in citrate agar, pH 6.0; similarly, the abnormal β-globin chain does not separate from β-A in urea 2-mercaptoethanol buffers of pH 8.9, but it moves anodically to β-A at pH 6.0. Peptide chromatography and amino acid analysis of the β chain reveal that the C-terminal histidine residue (β146) has been replaced by leucine. Like several other hemoglobins substituted at this residue, Hb Cowtown has a high oxygen affinity and a diminished Bohr effect.Keywords
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