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'Enzyme Induction' in keywords Facet   section ZfN Section C  [X]
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1999 (1)
1985 (1)
1983 (1)
1Author    Joachim Leube, Hans GrisebachRequires cookie*
 Title    Further Studies on Induction of Enzymes of Phytoalexin Synthesis in Soybean and Cultured Soybean Cells  
 Abstract    The glucan elicitor from cell walls o f the fungal pathogen, Phytophthora m egasperm a f. sp. glycinea, caused a decrease in activity o f 3-hydroxy-3-m ethylglutaryl coenzym e A reductase in wounded soybean cotyledons, whereas wounding alone led to an increase in the activity o f this enzyme. A decrease o f HM G -CoA reductase activity after elicitor treatment was also found in soybean hypocotyls and soybean cell cultures. In contrast to the activity o f H M G -CoA reductase, the activity o f dim ethylallylpyrophosphate: 3,6a,9-trihydroxypterocarpan dimethylallyltransferase increases after elicitor challenge o f soy­ bean cell cultures and after inoculation o f soybean hypocotyls (cv A m so y 7 1) with m ycelium o f either race 1 (incom patible) or race 3 (com patible) o f P. megasperma. 
  Reference    Z. Naturforsch. 38c, 730 (1983); received June 23 1983 
  Published    1983 
  Keywords    Phytoalexins, Soybean, Soybean Cell Cultures, Enzyme-Induction 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0730.pdf 
 Identifier    ZNC-1983-38c-0730 
 Volume    38 
2Author    Herman Clijsters, Ann Cuypers, Jaco VangronsveldRequires cookie*
 Title    Physiological Responses to Heavy Metals in Higher Plants; Defence against Oxidative Stress  
 Abstract    Depending on the physiological process investigated heavy metal phytotoxicity can be either inhibitory or stimulatory. Photosynthesis and its partial light and dark reactions are inhibited; the activity of various enzymes, located in several cell compartiments, is increased. These enzymes are mostly induced since metals affect the transcription activity. They appear to be related to the plant defence against oxidative stress caused by metal phytotoxicity. Careful examination of the time course of this induction reveals differences in response between the metals applied. 
  Reference    Z. Naturforsch. 54c, 730—7 (1999); received November 22 1998/April 10 1999 
  Published    1999 
  Keywords    Heavy Metals, Photosynthesis, Enzyme Induction, Oxidative Stress, Plant Defence Mechanisms 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0730.pdf 
 Identifier    ZNC-1999-54c-0730 
 Volume    54 
3Author    A. P. Singh, J. B. SinghRequires cookie*
 Title    Regulation of ß-Galactosidase Synthesis in Wild Type and in a Succinate-Resistant Mutant of Rhizobium meliloti  
 Abstract    The synthesis o f /?-galactosidase in Rhizobium m eliloti W U 60 was found to be inducible by lactose and its non-m etabolizable analogue, isopropyl-ß-D-thiogalactoside (IPTG). In contrast to Escherichia coli, galactose and m elibiose were very weak inducers o f this enzyme in R. meliloti. The maximum level o f /3-galactosidase in this bacterium is 2% o f that in fully induced E. coli. In addition to glucose, the induced synthesis o f this enzyme in R. m eliloti was repressed by galactose, glycerol, and succinate. In comparison to E. coli, addition o f cyclic AMP to the growth medium o f R. m eliloti did not alleviate the repressive effect o f the above com pounds on ß-galactosidase synthesis. High concentrations o f sodium succinate (100 m M) were inhibitory to the growth o f R. meliloti. Spontaneous succinate-resistant mutants could be isolated at low frequency. In contrast to the wild type parent, in a succinate-resistant mutant, the synthesis o f /J-galactosidase was not repressed by succinate. 
  Reference    Z. Naturforsch. 40c, 170—175 (1985); received October 3 1984 
  Published    1985 
  Keywords    /3-Galactosidase, Rhizobium meliloti, Enzyme Induction, Catabolite Repression, Succinate-Resistant Mutant 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0170.pdf 
 Identifier    ZNC-1985-40c-0170 
 Volume    40