Circular dichroism of aggregated deoxyhemoglobin S and the effect of amino acids.
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Biomedical subjects
Publications and source records attributed to D L Jue.
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A hemoglobin mutant with the mobility of hemoglobin (Hb) A on alkaline cellulose acetate or starch gel electrophoresis and mobility between Hb A and Hb S on citrate agar electrophoresis was detected in a patient with erythrocytosis. Structural analysis shows a substitution of histidine by tyrosine at position 145 in the beta-chain.
A new hemoglobin mutant was detected as a fast-moving variant on cellulose acetate electrophoresis at pH 8.4. The mutation is in the alpha-chain at position 127, where lysine is substituted by asparagine. This is an external residue, and mutation at this site does not lead to any altered physiologic function of the hemoglobin.
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