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Inhibition of rabbit skeletal muscle phosphorylase phosphatase by spermine

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Summary

The effect of three naturally occurring polyamines (putrescine, spermidine, and spermine) on the activity of rabbit skeletal muscle phosphorylase phosphatase was investigated. Only spermine significantly inhibited the enzyme. The mode of inhibition (Ki value of 0.3mm) of the phosphatase by spermine appears to be different from that caused by divalent metal ions or by other organic cations, such as arginine and lysine esters, since it is noncompetitive with respect to the substrate, phosphorylasea.

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Authors and Affiliations

  1. Section on Physiological Controls, Laboratory of Biomedical Sciences, National Institute of Child Health and Human Development, National Institutes of Health, 20014, Bethesda, Maryland, USA

    Chiharu Nakai & Walter Glinsmann

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  1. Chiharu Nakai
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  2. Walter Glinsmann
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Nakai, C., Glinsmann, W. Inhibition of rabbit skeletal muscle phosphorylase phosphatase by spermine. Mol Cell Biochem 15, 141–143 (1977). https://doi.org/10.1007/BF01793336

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  • DOI: https://doi.org/10.1007/BF01793336

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