Abstract
Adenosine monophosphate deaminase (AMPD) catalyzes the deamination of AMP to inosine monophosphate (IMP) with the subsequent liberation of ammonia. This reaction is part of the purine nucleotide cycle (Zöllner et al. 1993). Decreased activities of the muscle isoform of AMPD (myoadenylate deaminase, MAD) in man were first described in 1962 by Pennington from muscle biopsies of five patients with Duchenne-type muscular dystrophy. Two years later, reduced activities were found in a patient with periodic hypokalemic paralysis (Engel et al. 1964). Histochemical staining for AMPD was developed in 1978. Using this technique, five patients with muscle weakness or cramping were found whose muscle biopsies were normal except for a lack of MAD activity. MAD deficiency was therefore postulated as causing a metabolic myopathy with exercise-related symptoms (Fishbein et al. 1978).
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Gross, M. (1993). The Genetic Basis of Myoadenylate Deaminase Deficiency in Man. In: Gresser, U. (eds) Molecular Genetics, Biochemistry and Clinical Aspects of Inherited Disorders of Purine and Pyrimidine Metabolism. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84962-6_18
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DOI: https://doi.org/10.1007/978-3-642-84962-6_18
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