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A component of polyphloretin phosphate (PPP) may be an alternative substrate for ATP-glycerol transferase

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Summary

A low molecular weight fraction of a polyphloretin phosphate (PPP) preparation simulated glycerol in a milieu designed for enzymatic assay of glycerol. It is suggested that a component of this PPP mixture is able to act as an alternative substrate for the ATP-glycerol transfer enzyme; it becomes phosphorylated and thus initiates the series of reactions resulting in a increased conversion of NADH to NAD and the observed changes in absorbance.

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Author notes

  1. P. B. Curtis-Prior

    Present address: Unit for Metabolic Diseases, Synthelabo-LERS, 31, Avenue Paul Vaillant-Couturier, F-92220, Bagneux, France

Authors and Affiliations

  1. Metabolic and Nutrition Unit, Research Department, The Marie Curie Memorial Foundation, Oxted, (Surrey), UK

    P. B. Curtis-Prior & Marilynn Jenner

Authors
  1. P. B. Curtis-Prior
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  2. Marilynn Jenner
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Additional information

The authors are pleased to acknowledge the support of Dr D.C. Williams, the useful discussion with Dr M. Higgins and Dr J.J.M. Rowe and the generous supply of polyphloretin compounds from A.B. LEO Laboratories, Helsingborg, Sweden.

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Curtis-Prior, P.B., Jenner, M. A component of polyphloretin phosphate (PPP) may be an alternative substrate for ATP-glycerol transferase. Experientia 37, 335–336 (1981). https://doi.org/10.1007/BF01959846

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  • DOI: https://doi.org/10.1007/BF01959846

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