caa a22 4500 477100872 CHVBK 20180405111541.0 cr unu---uuuuu 170330e19960901xx s 000 0 eng 10.1007/BF00620052 doi (NATIONALLICENCE)springer-10.1007/BF00620052 Glutathione synthesis in maize genotypes with different sensitivities to chilling [Elektronische Daten] [Gábor Kocsy, Monika Brunner, Adrian Rüegsegger, Peter Stamp, Christian Brunold] The effect of chilling on enzymes, substrates and products of sulfate reduction, gultathione synthesis and metabolism was studied in shoots and roots of maize (Zea mays L.) genotypes with different chilling sensitivity. At full expansion of the second leaf, chilling at 12 °C inhibited dry weight increase in shoots and roots compared to controls at 25 °C and induced an increase in adenosine 5′-phosphosulfate sulfotransferase and γ-glutamylcysteine synthetase (EC 6.3.2.2) activity in the second leaf of all genotypes tested. Glutathione synthetase (EC 6.3.2.3) activity was about one order of magnitude higher than γ-glutamylcysteine synthetase activity, but remained unchanged during chilling except for one genotype. During chilling, cysteine and glutathione content of second leaves increased to significantly higher levels in the two most chilling-tolerant genotypes. Comparing the most tolerant and most sensitive genotype showed that chilling induced a greater incorporation of35S from [35S]sulfate into cysteine and glutathione in the chilling-tolerant than in the sensitive genotype. Chilling decreased the amount of35S-label incorporated into proteins in shoots of both genotypes, but had no effect on this incorporation in the roots. Glutathione reductase (EC 1.6.4.2) and nitrate reductase (EC 1.6.6.1) activity were constitutively higher in the chilling-tolerant genotypes, but showed no changes in most examined genotypes during 3 d at 12 °C. Our results indicate that in maize glutathione is involved in protection against chilling damage. Springer-Verlag, 1996 Chilling nationallicence Glutathione synthesis nationallicence Sulfate reduction Zea nationallicence APSSTase : adenosine 5′-phosphosulfate sulfotransferase nationallicence γEC : γ-glutamylcysteine nationallicence GR : glutathione reductase nationallicence OSH : glutathione nationallicence NR : nitrate reductase nationallicence Kocsy Gábor Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut Brunner Monika Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut Rüegsegger Adrian Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut Stamp Peter Institute of Plant Sciences, ETH Zurich, Universitätsstrasse 2, CH-8092, Zürich, Switzerland aut Brunold Christian Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut Planta Springer-Verlag 198/3(1996-09-01), 365-370 0032-0935 198:3<365 1996 198 425 https://doi.org/10.1007/BF00620052 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00620052 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kocsy Gábor Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut NATIONALLICENCE 700 1- Brunner Monika Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut NATIONALLICENCE 700 1- Rüegsegger Adrian Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut NATIONALLICENCE 700 1- Stamp Peter Institute of Plant Sciences, ETH Zurich, Universitätsstrasse 2, CH-8092, Zürich, Switzerland aut NATIONALLICENCE 700 1- Brunold Christian Institute of Plant Physiology, University of Berne, Altenbergrain 21, CH-3013, Berne, Switzerland aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/3(1996-09-01), 365-370 0032-0935 198:3<365 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer