, Volume 189, Issue 4, pp 561–566

Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension

  • Christiane Paulus
  • Barbara Köllner
  • Hans-Jörg Jacobsen

DOI: 10.1007/BF00198220

Cite this article as:
Paulus, C., Köllner, B. & Jacobsen, HJ. Planta (1993) 189: 561. doi:10.1007/BF00198220


Using a strictly auxin-dependent soybean (Glycine max (L.) Merr.) cell suspension, we studied the correlation of auxin-dependent cell proliferation and the activity of glyoxalase I (S-lactoylglutathione-lyase EC, an enzyme generally associated with cell proliferation in animal, microbial and, as reported recently, also plant systems. We found the activity of glyoxalase I to be modulated during the proliferation cycle, with a maximal activity between day 2 and day 4 of culture growth. After starving the culture of auxins for three subsequent periods, both the enzyme activity and cell growth could be re-initiated with auxin. Enzyme activity reached its maximum 1 d before cell number was at a maximum. The enzyme was purified to homogeneity and characterized.

Key words

Auxin Enzyme induction Glycine (cell suspension) Glyoxalase I (purification) 



2,4-dichlorophenoxyacetic acid


reuced glutathione


relative molecular mass


polyacrylamide gel electrophoresis


sodium dodecyl sulfate

Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Christiane Paulus
    • 1
  • Barbara Köllner
    • 1
  • Hans-Jörg Jacobsen
    • 2
  1. 1.Institute of GeneticsUniversity of BonnBonn 1Germany
  2. 2.Department of Molcular GeneticsUniversity of HannoverHannoverGermany

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