Studies on the Oxidation-Reduction Potentials of Heme Proteins

In the preceding paper of this series (1) we reopened the study of the oxidation-reduction potentials of normal hemoglobin, taking up the subject where it had been left by Taylor and Hastings (2) and by Havemann (3) nearly 20 years ago. These earlier investigators had studied horse and ox hemoglobin, respectively, and limited themselves to the dye titration method. Our work was on human hemoglobin, and in addition to the dye titration method we made use of the method of mixtures. (Both of these methods are explained below.) As regards the absolute values of Et’ and the Bohr effect, our results are in close agreement with the earlier observations on horse hemoglobin; on the other hand, as regards the shape of the equilibrium curves and the way in which the shape changes with pH, we obtained different results, which varied with the method. Our curves obtained by the method of mixtures are all symmetrical with values of n as high as 2.6 at alkaline pH, although the value of n depends somewhat on the way in which the ferrihemoglobin employed is made. In contrast, the curves obtained by the dye titration method are always more or less asymmetrical. In all cases la drops towards 1 (about 1.2) at low pH. We believe that the method of mixtures, in which the possibility of the binding of dye by the protein is eliminated, is the more reliable. In the present study we extend the measurements of oxidation-reduction potentials to derivatives of normal human hemoglobin obtained by digestion with carboxypeptidases A and B. These are: HbCPA,2 in which the two COOH-terminal residues, tyrosine and histidine, occupying positions 145 and 146 of the /3 chains, have been removed by the action of carboxypeptidase A; HbCPB, in which the COOH-terminal residue,

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  2003

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  DOI 10.1016/s0021-9258(18)51676-8
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