title: Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension.
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), 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.
authors.affiliation: Institute of Genetics, University of Bonn, FRG.
authors.forename: C
authors.initials: C
authors.lastname: Paulus
authors.forename: B
authors.initials: B
authors.lastname: Köllner
authors.forename: H J
authors.initials: HJ
authors.lastname: Jacobsen
mesh_terms: 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
chemical_list: D007210:Indoleacetic Acids; D007791:Lactoylglutathione Lyase