Abstract
THE reactivity of the sulphydryl groups of human hæmoglobin has been examined in many laboratories. Recently, Cecil and Snow1 have reported spectral changes in 6 M urea at pH 9 when 8 equivalents of HgCl2 are added to oxyhæmoglobin (HbO2) and metHb at 37° C. In the course of investigations in this Laboratory on the effect of HgCl2, it was observed that the addition of more than 10 equivalents of mercury per hæmoglobin produces marked changes in the absorption spectra and the rotatory dispersion curves of both HbO2 and metHb. The final product, in both instances, is similar to acid-denatured protein. Hardman and Gurd2 have made essentially the same observations when copper or zinc reacts with metmyoglobin.
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References
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RESNIK, R. Interaction of Mercuric Ion with Hæmoglobin. Nature 203, 880–882 (1964). https://doi.org/10.1038/203880a0
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DOI: https://doi.org/10.1038/203880a0
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