Abstract
GENETIC variants of several mammalian cell lines which are not able to incorporate preformed purine or nucleoside into the cell's nucleic acids have been known for some time. In some of these cell lines a lack of activity of the enzyme inosinic pyrophosphorylase (IPP), also called hypoxanthine-guanine phosphoribosyltransferase (PRT) (EC 2.4.2.8), has been demonstrated1–4. This enzyme catalyses the conversions both of hypoxanthine to inosinic acid and of guanine to guanylic acid, and constitutes an essential part of one of the purine “salvage” pathways. Seegmiller and his colleagues5 have recently shown that the severe sex-linked neurological disease of humans known as the Lesch–Nyhan syndrome is associated with the virtual complete absence of this enzyme activity from brain and all other tissues which have been examined6.
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FRIEDMANN, T., SEEGMILLER, J. & SUBAK-SHARPE, J. Metabolic Cooperation between Genetically Marked Human Fibroblasts in Tissue Culture. Nature 220, 272–274 (1968). https://doi.org/10.1038/220272a0
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DOI: https://doi.org/10.1038/220272a0
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