Metabolism of AMP in Muscle Extracts from Patients with Deficient Activity of Myoadenylate Deaminase

  • Kari O. Raivio
  • Pirkko Santavuori
  • Hannu Somer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 165)


In a number of patients with muscle weakness, cramps, and easy fatigability, deficient activity of adenylate deaminase (AMPD) in muscle tissue has been demonstrated1,2. The enzyme defect seems to be correlated with failure to release ammonia from muscle during exercise. Since a simultaneous depletion of adenine nucleotides in muscle tissue has been detected, disruption of the purine nucleotide cycle has been postulated as the pathogenetic mechanism. This hypothesis, however, fails to account for the problem, how deficiency of a catabolic enzyme can result in substrate depletion. Furthermore, association of AMPD-deficiency with variable clinical conditions has raised doubts about the primary role of the enzyme defect2,4.


Double Reciprocal Plot Hypoxanthine Phosphoribosyltransferase Deficient Activity Easy Fatigability Purine Nucleotide Cycle 


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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Kari O. Raivio
    • 1
  • Pirkko Santavuori
    • 1
  • Hannu Somer
    • 1
  1. 1.Children’s Hospital, Department of Obstetrics and Gynecology, and of NeurologyUniversity of HelsinkiHelsinki 29Finland

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