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'Elicitors' in keywords Facet   Publication Year 1995  [X]
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1995[X]
1Author    Kohki Akiyamaa, Kazuyoshi Kawazua, Akio KobayashibRequires cookie*
 Title    Partially N-Deacetylated Chitin Oligomers (Pentamer to Heptamer) are Potential Elicitors for (+)-Pisatin Induction in Pea Epicotyls  
 Abstract    Oligomers (dimer to heptamer) of chitosan and their partially/completely N-acetylated derivatives were examined for (+)-pisatin-inducing activities in pea epicotyl elicitor assay at concentrations ranging from 6.25 to 100 j.ig/ml. The structures of the oligomers were analyzed by 'H NM R and M A L D I TOF MS spectrometers. The chitosan oligomers from dimer to tetramer were inactive, while the pentamer exhibited a moderate activity at 100 |ig/ml. The hexamer showed a pronounced activity at 100 |ag/ml, whereas the oligomer had no activity at the higher concentrations. Although the chitosan heptamer induced a moderate amount of (+)-pisatin (ca. 60 j.ig/g fr. wt.) at 50 (.ig/ml, the oligomer did not elicit pisatin formation at 100 |ig/ml. The dimer to tetramer of both partially N-deacetylated chitin (DAC) and chitin were totally inactive. The DAC pentamers (d.a. 31%, 52%), DAC hexamers (d.a. 26%, 41%), and DAC heptamers (d.a. 26%, 36%) exhibited significant elicitor activities at lower concen­ trations (6.25-25 [.ig/ml) than the native chitosan oligomers. The chitin pentamer to heptamer had weak or no activity. Both glucosamine and N-acetylglucosamine were inactive in the assay. These facts suggest that the DAC pentamer to heptamer may act as elicitors for pisatin induction in pea-fungus interactions. 
  Reference    Z. Naturforsch. 50c, 391—397 (1995); received January 4/January 15 1995 
  Published    1995 
  Keywords    Elicitor, Chitosan, Chitin, Phytoalexin, Pisum sativum 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0391.pdf 
 Identifier    ZNC-1995-50c-0391 
 Volume    50 
2Author    Claudia Biicker, Barbara Witte, Ursula Windmiillera, HansJ. GrambowRequires cookie*
 Title    Anthranilate Synthase and Chorismate Mutase Activities in Stem Rust-Inoculated and Elicitor-Treated Resistant, Moderately Resistant, and Susceptible Near-Isogenic Wheat Lines  
 Abstract    Anthranilate synthase and chorismate mutase activities which control the flow of substrate from chorismate into the tryptophan pathway and into the phenylalanine/tyrosine pathway, respectively, were examined in three near isogenic wheat lines of Triticum aestivum L. (cv. Prelude Sr5, highly resistant to stem rust infection; cv. Prelude Sr24, moderately resistant; cv. Prelude srx, susceptible). The activities of both enzymes were found to increase in re­ sponse to inoculation with the stem rust fungus Puccinia graminis f. sp. tritici or treatment with Pgt elicitor. Thus, both the tryptophan branch and the phenylalanine branch appear to contribute to the resistance response in wheat leaves. Only the cytosolic but not the plastidic fraction of the enzyme activities appears to be affected by fungal infection or elicitor treat­ ment. Some differences with respect to degree and time dependency of enzyme activation were noticed between the three wheat lines following inoculation but not after treatment with the Pgt elicitor. 
  Reference    Z. Naturforsch. 50c, 54 (1995); received September 7/October 21 1994 
  Published    1995 
  Keywords    Anthranilate Synthase, Chorismate Mutase, Elicitor, Triticum aestivum, Puccinia graminis 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0054.pdf 
 Identifier    ZNC-1995-50c-0054 
 Volume    50