Evidence for absence of an interaction between purified 3-phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase

Mária Vas, József Batke

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The possibility of a functional complex formation between glyceraldehyde-3-phosphate dehydrogenase (EC and 3-phosphoglycerate kinase (EC, enzymes catalysing two consecutive reactions in glycolysis has been investigated. Kinetic analysis of the coupled enzymatic reaction did not reveal any kinetic sign of the assumed interaction up to 4 · 10-6 M kinase and 10-4 M dehydrogenase. Fluorescence anisotropy of 10-7 M or 2 · 10-5 M glyceraldehyde-3-phosphate dehydrogenase labeled with fluorescein isothiocynate did not change in the presence of non-labeled 3-phosphoglycerate kinase (up to 4 · 10-5 M). The frontal gel chromatographic analysis of a mixture of the two enzymes (10-4 M dehydrogenase and 10-5 M kinase) could not reveal any molecular species with the kinase activity having a molecular weight higher than that of 3-phosphoglycerate kinase. Both types of physicochemical measurements were also performed in the presence of substrates of the kinase and gave the same results. The data seem to invalidate the hypothesis that there is a complex between purified pig muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase.

Original languageEnglish
Pages (from-to)193-198
Number of pages6
JournalBBA - Enzymology
Issue number2
Publication statusPublished - Aug 13 1981



  • 3-Phosphoglycerate kinase
  • Enzyme-enzyme interaction
  • Glyceraldehyde-3-phosphate dehydrogenase

ASJC Scopus subject areas

  • Medicine(all)

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