Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension
- 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 126.96.36.199.), 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 wordsAuxin Enzyme induction Glycine (cell suspension) Glyoxalase I (purification)
relative molecular mass
polyacrylamide gel electrophoresis
sodium dodecyl sulfate