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• W33420487 abstract "SUMMARY The tyrosines were titrated adding KOH or HCl to the pro- tein solutions in 0.25 M NaCl at 20”. Their ionization was followed by differential spectrophotometry at 245 rnp against a reference solution at pH 8.5. The titrations were reversible only up to pH 10.5. The back titrations from pH 12 indicated that the denaturation of the protein produced a change in the absorption spectrum of the heme in the ultraviolet region. Making correction for this transition, the AC per tyrosyl residue was calculated to be approximately 10,000 for all of the proteins investigated. Considering that only 2 out of 3 tyrosyl residues per chain ionize in the native proteins and neglecting the correction for the electrostatic interaction, the reversible part of the titrations was shown to be consistent with pK near 10.4 for hemoglobin, apohemoglobin, and the 0 chains, with pK near 9.9 for the OL chains. This difference was too large to be accounted for on the basis of the electrical charge of the various proteins. It could indicate a difference in the ionization of the tyrosyl residues of the 01 chains when these are isolated or polymerized with the ,l3 chains in the hemoglobin molecule. In a recent paper detailed comparison was made of the proton- binding behavior of hemoglobin, its isolated subunits, and apohe- moglobin. There it was shown how the (r-p interaction and the heme-globin interaction affects the titration of the histidyl and lysyl residues in hemoglobin (I). The number of tyrosyl residues was too few in comparison to other classes of ionizable groups and with a too high pK in order to have a recognizable influence on the acid-base titration of hemoglobin, which was extended only up to pH 10.4. On the other hand, their ionization can be specifically measured with the spectrophotometer. Many data already exist in the litera- ture on this subject (2-4). Unfortunately, they were all obtained in the presence of buffers of various kinds so they * This work was supported in part by National Institute of Health Grants HE 10785-02 and HE 06308. $ To whom requests for reprints should be addressed. should have been corrected in order to be translated into our experimental conditions. No back titrations are available in the literature so it was impossible to know whether the pK values reported were for the native or for the alkali-denatured protein, and no titrations have been carried out on the isolated cr chains or on native apohemoglobin. For these reasons we felt it neces- sary to reinvestigate the problem starting from the very begin- ning in order to study the effect of the c@ interaction and of the heme-apohemoglobin interaction on the ionization of the tyrosyl residues in hemoglobin." @default.
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• W33420487 date "1968-11-01" @default.
• W33420487 modified "2023-09-30" @default.
• W33420487 title "Protonation of Tyrosyl Residues in the Carboxy Derivatives of Hemoglobin, Its Isolated Subunits, and Apohemoglobin" @default.
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• W33420487 doi "https://doi.org/10.1016/s0021-9258(18)94512-6" @default.
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