Abstract
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 4.4.1.5.), 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.
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Abbreviations
- 2,4-D:
-
2,4-dichlorophenoxyacetic acid
- GSH:
-
reuced glutathione
- Mr:
-
relative molecular mass
- PAGE:
-
polyacrylamide gel electrophoresis
- SDS:
-
sodium dodecyl sulfate
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The authors thank Dr. K. Palme, Max-Planck-Institute, Cologne, for reverse-phase chromatography. Part of this work was done by C. Paulus at the Department of Biotechnology, New Delhi, India under the Bundesministerium für Forschung und Technologie (BMFT)-funded Indo-FRG collaboration programme. Thanks are due to Professors S. Guha-Mukherjee and S.K. Sopory, New Delhi, for introduction into glyoxalase research. The research was funded by a BMFT-DECHEMA fellowship to C. Paulus, a BMFT grant to H.-J. Jacobsen and a Graduierten Förderung des Landes Nordrhein-Westfalen fellowship to B. Köllner.
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Paulus, C., Köllner, B. & Jacobsen, HJ. Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension. Planta 189, 561–566 (1993). https://doi.org/10.1007/BF00198220
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DOI: https://doi.org/10.1007/BF00198220