Abstract
THE structural alteration of mammalian hæmoglobin on ageing in vivo is evidenced by the accelerated electro-phoretic mobility of older hæmoglobin1 and its changed chromatographic behaviour2. Hybridization investigations have shown the variant chain in old hæmoglobin to be the β-chain3. A number of suggestions have been made as to the possible chemical nature of the modification4, the main one being that mixed disulphide formation with glutathione occurs5,6 as a consequence of the diminished enzyme activities present in older red blood cells.
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WALTER, H., SELBY, F. Chemical Reactivity of Avian and Mammalian Hæmoglobins of Different Ages. Nature 204, 1209–1210 (1964). https://doi.org/10.1038/2041209a0
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DOI: https://doi.org/10.1038/2041209a0
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