Abstract
IT has previously been shown in this laboratory1 that at least two liver factors are necessary for the oxidation of D-ribose-5-phosphate by ammonium sulphate precipitated fractions of horse or rat liver, one being an aldolase and the other a dehydrogenase specific for coenzyme II. Ribose-5-phosphate is oxidized most rapidly by a combination of liver fractions A (0.4–0.5 saturation with ammonium sulphate) and B (0.5–0.6 saturation), the former being richest in glucose-6-phosphate dehydrogenase and the latter most active in splitting ribose-5-phosphate, as judged by the disappearance of pentose using the orcinol method2. The breakdown of ribose-5-phosphate, unlike the oxidation, is independent of coenzyme II and oxygen and never proceeds beyond 66–72 per cent disappearance of pentose.
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GLOCK, G. Formation and Breakdown of Pentose Phosphates by Liver Fractions. Nature 170, 162–163 (1952). https://doi.org/10.1038/170162b0
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DOI: https://doi.org/10.1038/170162b0
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