Quaternary structure of higher plant glyceraldehyde-3-phosphate dehydrogenases

Eur J Biochem. 1979 Feb 15;94(1):243-7. doi: 10.1111/j.1432-1033.1979.tb12891.x.


1. NAD(P)+-induced changes in the aggregational state of prepurified NADP-linked glyceraldehyde-3-phosphate dehydrogenase (EC were used to isolate the enzyme from Spinacia oleracea, Pisum sativaum and Hordeum vulgare. Each of the three plant species contains two separate isoenzymes. Isoenzyme 1 (fast moving during conventional electrophoresis) precipitates with the ammonium sulfate fraction 55--70% saturation. It shows two separate subunits in dodecylsulfate gels, which are probably arranged as A2B2 in the native enzyme molecule. Isoenzyme 2 (slow moving during conventional electrophoresis) precipitates with the ammonium sulfate fraction 70--95%. It contains a sigle subunit of the same Mr as subunit A in isoenzyme 1 and is apparently a tetramer (A4). The molecular weights of subunits A/B for spinach, peas and barley were determined as 38,000/40,000, 38,000/42,000 and 36,000/39,000 respectively. 2. The NAD-specific glyceraldehyde-3-phosphate dehydrogenase (EC was purified from Spinacia oleracea and Pisum sativum by affinity chromatography on blue Sepharose CL-6B. The enzyme from both plant species is shown to be a tetramer of subunits with Mr 39,000. 3. The present findings contrast with heterogeneous results obtained previously by other authors. These results suggested that there are considerable interspecific differences in the quaternary structure of glyceraldehyde-3-phosphate dehydrogenases from higher plants.

Publication types

  • Comparative Study

MeSH terms

  • Glyceraldehyde-3-Phosphate Dehydrogenases* / isolation & purification
  • Macromolecular Substances
  • NAD / metabolism
  • NADP / metabolism
  • Peptides / analysis
  • Plants / enzymology*
  • Protein Conformation
  • Species Specificity


  • Macromolecular Substances
  • Peptides
  • NAD
  • NADP
  • Glyceraldehyde-3-Phosphate Dehydrogenases