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Inactivation of phosphoglycerate mutase and creatine kinase isoenzymes in human serum
  1. N Durany1,
  2. J Carreras2,
  3. M Valentí2,
  4. J Cámara2,
  5. J Carreras2
  1. 1Health Science Faculty, International University of Catalunya, Gomera s/n, 08190-St Cugat del Vallés, Barcelona, Spain
  2. 2Unit of Biochemistry and Molecular Biology, Faculty of Medicine, Institut d’Investigacions Biomédiques August Pi I Sunyer (IDIBAPS), University of Barcelona, Casanova, 143, 08036-Barcelona, Spain
  1. Correspondence to:
 Professor J Carreras, Unit of Biochemistry and Molecular Biology, Faculty of Medicine, University of Barcelona, Casanova, 143, Barcelona-08036, Spain;
 jcarrera{at}medicina.ub.es

Abstract

Aims/Background: Total phosphoglycerate mutase (PGM) activity in serum has been shown to be increased in acute myocardial infarction with the same time course as creatine kinase (CK) activity. However, the increase in the muscle (MM) and in the cardiac (MB) PGM isoenzymes was not as high as expected. The present study was undertaken to characterise PGM inactivation by serum and to compare it with serum CK inactivation.

Methods: The PGM and the CK activities of extracts of human heart, skeletal muscle, and brain were determined spectrophotometrically after incubation with different media, namely: plasma, whole serum, dialysed serum, heated serum, serum ultrafiltrate, urate solution, and buffer solution.

Results: Type MM PGM was inactivated by plasma, whole serum, heated serum, dialysed serum, and serum ultrafiltrate. Inactivation in dialysed serum was reduced by EDTA and largely reversed by thiol agents. Inactivation in serum ultrafiltrate was not prevented by EDTA and only partially reversed by dithiothreitol. The muscle and type BB CK isoenzymes were inactivated in all the tested media. The incubation of human and rabbit skeletal muscle PGM and CK in urate solution showed that urate does not affect mutase activity under conditions that inactivate CK.

Conclusions: These results confirm the mechanisms of CK inactivation proposed by others and show that the type M PGM subunit is inactivated by two different mechanisms, which appear to involve the thiol groups of the enzyme. One mechanism is caused by either a protein component or a protein bound serum component and involves calcium ions and/or another chelatable metal ion. The other mechanism is caused by a lower molecular weight serum component and is metal ion independent.

  • creatine kinase
  • inactivation by serum
  • phosphoglycerate mutase
  • CK, creatine kinase
  • DTT, dithiothreitol
  • PGM, phosphoglycerate mutase

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