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Muscle phosphoglycerate rnutase deficiency

H. Houston Merritt Clinical Research Center for Muscular Dystrophy and Related Diseases, Columbia University College of Physicians and Surgeons (Drs. DiMauro, Miranda, Olarte, and Hays), and the Department of Medicine, New York University (Dr. Friedman).

A 52-year-old man complained since adolescence of cramps and pigmenturia after 15 to 30 minutes of intense exercise. There was no family history of neuromuscular diseases, and strength was normal. The rise of venous lactate after forearm ischemic exercise was abnormally low. Histochemical and ultrastructural studies of a muscle biopsy showed mild increase of glycogen, which was confirmed by biochemical analysis. Studies of anaerobic glycolysis in vitro showed decrease lactate formation with glycogen and with all hexosephosphate glycolytic intermediates, suggesting a defect below the phosphofructokinase reaction. Muscle phosphoglycerate mutase (PGAM) activity was 5.7% of the lowest control, while all other enzymes of glycolysis had normal activities. Electrophoretic, heat lability, and mercury inhibition studies showed that the small residual activity of PGAM in the patient's muscle was represented by the brain (BB) isoenzyme, suggesting a genetic defect of the M subunit that predominates in normal muscle. The prevalence of the BB isoenzyme in other tissues, including muscle culture, may explain why symptoms were confined to muscle.

Address correspondence and reprint requests to Dr. DiMauro, 4–420 College of Physicians and Surgeons, 630 W. 168th Street, New York, NY 10032.

Supported by Center Grants NS-11766–08 from the National Institute of Neurological and Communicative Disorders and Stroke, from the Muscular Dystrophy Association, and by grant AM-25500-03 from the National Institute of Arthritis, Metabolism, and Digestive Diseases.

Accepted for publication November 4, 1981.

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