Phosphoglycerate kinase deficiency myopathy: Biochemical and immunological studies of the mutant enzyme

N. Bresolin, A. Miranda, H. W. Chang, S. Shanske, S. DiMauro

Research output: Contribution to journalArticle


A new phosphoglycerate kinase variant (PGK New Jersey) has been purified from muscle and cultured fibroblasts of a patient with recurrent myoglobulinuria. The mutant enzyme had higher than normal affinity for adenosine triphosphate (ATP) and 3-phosphoglycerate, and a shift of the pH optimum towards the acidic side. Antibodies raised against PGK purified from normal muscle were used to evaluate the presence of immunologically cross-reacting enzyme protein in tissues from the patient. Immunodiffusion and an antibody consumption test showed the presence of reduced amounts of cross-reacting material in the patient's muscle. Several PGK variants have been characterized in asymptomatic individuals or in patients with hemolytic anemia. The biochemical features of PGK New Jersey, the only known variant associated with recurrent myoglobulinuria, distinguish this mutant enzyme from others.

Original languageEnglish
Pages (from-to)542-551
Number of pages10
JournalMuscle and Nerve
Issue number7
Publication statusPublished - 1984


ASJC Scopus subject areas

  • Clinical Neurology
  • Neuroscience(all)

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