Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension.
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), and 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.
Paulus
C
C
Institute of Genetics, University of Bonn, FRG.
Köllner
B
B
Jacobsen
H J
HJ
D002455:Cell Division; D002478:Cells, Cultured; D004790:Enzyme Induction; D007210:Indoleacetic Acids / Q000502:physiology; D007791:Lactoylglutathione Lyase / Q000096:biosynthesis / Q000302:isolation & purification / Q000502:physiology*; D008969:Molecular Sequence Data; D013025:Glycine max / Q000166:cytology / Q000201:enzymology
D007210:Indoleacetic Acids; D007791:Lactoylglutathione Lyase