Human muscle phosphoglycerate mutase deficiency: newly discovered metabolic myopathy.

Abstract

Muscle phosphoglycerate mutase activity was decreased (5.7 percent of the lowest control value) in a 52-year-old man with intolerance for strenuous exercise and recurrent pigmenturia since adolescence. All of the other enzymes of glycolysis had normal activities, and glycogen concentration was normal. Electrophoretic, heat lability, and mercury inhibition studies showed that the small residual activity in the patient's muscle was represented by the brain (BB) isoenzyme of phosphoglycerate mutase, suggesting a genetic defect of the M subunit which predominates in normal muscle. The prevalence of the BB isoenzyme in other tissues, including muscle culture, may explain why symptoms were confined to muscle.

• Authors: S DiMauro, A F Miranda, S Khan, K Gitlin, R Friedman
• Journal: Science (New York, N.Y.) (Science) Vol. 212 Issue 4500 Pg. 1277-9 (Jun 12 1981) ISSN: 0036-8075 [Print] United States
• PMID: 6262916 (Publication Type: Case Reports, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Isoenzymes
• Phosphorylases
• Phosphotransferases
• Phosphoglycerate Mutase

Topics

• Brain (enzymology)
• Glycolysis
• Humans
• Isoenzymes (metabolism)
• Male
• Middle Aged
• Muscles (enzymology)
• Muscular Diseases (enzymology, genetics)
• Organ Specificity
• Phosphoglycerate Mutase (deficiency, metabolism)
• Phosphorylases (metabolism)
• Phosphotransferases (deficiency)
• Reference Values