Amino acid substitution (histidine to tyrosine) in a glucose-6-phosphate dehydrogenase variant (G6PD Hektoen) associated with over-production.
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Biomedical subjects
Publications and source records attributed to A Yoshida.
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Ribosome-bound peptides were prepared from rabbit reticulocytes incubated in a reaction mixture that contained all essential amino acids except tryptophan. The peptides were fractionated by Sephadex gel filtration and the N-termini of these peptides were examined. Longer uncompleted hemoglobin chains (larger than 30 amino acids) had unblocked valine at the N-terminal position. In contrast, shorter initial parts of chains (smaller than 16 amino acids) did not have valine at the N-terminal position. These small peptides had methionine at the N-terminal, and 8% of the terminal methionine was presumably formylated. These findings indicate that hemoglobin chains are initiated from methionine or N-formylmethionine (or from both methionine and N-formylmethionine), and that the methionyl residue is hydrolyzed at an early stage of chain elongation.
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The mechanism of alkali resistance in hemoglobin Rainier, an adult human hemoglobin variant (beta 145 tyrosinie --> histidinie), has been investigated. Alkali denaturation kinetics, electrophoretic and hybridization study. and ultracentrifuge analysis provided evidence for a monomeric beta Rainiier chain resisting denaturation at alkaline pH. These data provide evidence for a previously unrecognized effect of a single amino acid substitution, that is, the change of the alkali denaturation properties of monomneric chains.
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