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Phosphoglycerate kinase deficiency myopathy: Biochemical and immunological studies of the mutant enzyme
Author(s) -
Bresolin Nereo,
Miranda Armand,
Chang Hai Won,
Shanske Sara,
DiMauro Salvatore
Publication year - 1984
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880070705
Subject(s) - myoglobinuria , phosphoglycerate kinase , phosphoglycerate mutase , enzyme , microbiology and biotechnology , biochemistry , mutant , creatine kinase , adenosine triphosphate , myopathy , biology , antibody , mutation , chemistry , medicine , glycolysis , immunology , gene , rhabdomyolysis , genetics
A new phosphoglycerate kinase variant (PGK New Jersey) has been purified from muscle and cultured fibroblasts of a patient with recurrent myoglobinuria. 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 myoglobinuria, distinguish this mutant enzyme from others.