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The Characterization of Modified Human Hemoglobin

II. REACTION WITH 1-FLUORO-2,4-DINITROBENZENE

From the ¹ From the Department of Biochemistry, Yale University, New Haven, Connecticut 06520

A dinitrophenyl derivative of human hemoglobin has been prepared and purified, in which the only site of reaction is the NH₂ terminus of the chain. Evidence for this comes from two sources: first, the identification of all of the tryptic peptides having absorption at 355 mµ; second, from experiments with ¹⁴C-labeled 1-fluoro-2,4-dinitrobenzene which show that the stoichiometry of the reaction is 1 dinitrophenylgroup per ß subunit. Competition experiments with iodoacetamide show that 1-fluoro-2,4-dinitrobenzene does not react with the "reactive" sulfhydryl group on the ß chain.

This single substitution leads to quite drastic physical and functional changes. The modified hemoglobin has an increased oxygen affinity, an n value of 1 in the Hill equation, and no Bohr effect. In all dissociating solvents tested, the dinitrophenyl-hemoglobin is more highly associated than native hemoglobin.

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