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  • Electronic Resource  (2)
  • 1995-1999  (2)
  • 1985-1989
  • Meloidogyne javanica  (1)
  • Triticum aestivum  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Genetic resources and crop evolution 46 (1999), S. 557-568 
    ISSN: 1573-5109
    Keywords: Arachis spp. ; Meloidogyne javanica ; resistance ; root-knot nematodes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The root-knot nematode, Meloidogyne javanica Race 3 is an important nematode parasite of groundnut. Greenhouse evaluation of 184 accessions of 33 wild Arachis spp. five interspecific derivatives, 18 groundnut cultivars for root damage (galls formed by nematode) and nematode reproduction demonstrated that resistance to the nematode is available in the genepool of wild Arachis spp. Seven accessions, ICG 8952 (Arachis helodes), ICC 13211 (A. sylvestris), ICG 13224 (A. kretscmeri), ICG 13231 (Arachis sp.), ICG 14862 (A. kuhlmannii), ICG 14868 (A. stenosperma), and ICG 14915 (A. sylvestris) were highly resistant to nematode reproduction and root damage. There was no gall and eggmass formation on any plant of these accessions. Thirty-three accessions were resistant and 14 were moderately resistant. All the tested accessions of A. monticola, A. benensis, A. ipaensis, A. hoehnei, A. kempff-mercadoi, A. valida, A. chiquitana, A. rigonii, A. vallsii, A. dardani, A. paraguariensis, A. triseminata, interspecific derivatives, and groundnut cultivars were susceptible. The possible use of resistance sources in the breeding program is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthetica 36 (1999), S. 433-440 
    ISSN: 1573-9058
    Keywords: antibody ; polyacrylamide gel electrophoresis ; protease ; Triticum aestivum ; wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Exposure of thylakoid membranes to high temperature in dark leads to the degradation of D1 protein. Maximum degradation of D1 protein occurred at 45 °C. Using N-terminal specific D1 antibody, a 23 kDa fragment of D1 protein was detected. The degradation of D1 protein could be prevented both by radical scavengers and inhibitors of serine protease and metallo-protease. These results suggest that degradation of D1 protein during exposure of thylakoid membranes to high temperature in dark is catalyzed by protease.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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