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  • 1990-1994  (2)
  • 1960-1964
  • Agrotis segetum Schiff.  (1)
  • Brassica (protein targeting)  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of chemical ecology 20 (1994), S. 1063-1073 
    ISSN: 1573-1561
    Keywords: Oxime ether ; NMR data ; pheromone mimics ; ESG studies ; structure-response relationships ; turnip moth ; Agrotis segetum Schiff. ; Lepidoptera ; Noctuidae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Oxime ether analogs of sex pheromone components of the turnip moth (Agrotis segetum Schiff.) were synthesized by the acidolytic opening of cyclic enol ethers withO-alkyl hydroxylamine hydrochlorides. The compounds varying in chain lengths and in the position of the C=N double bond were studied by electrophysiological single sensillum recordings (electrosen-sillography: ESG). The ESG data indicate in general reduced receptor interaction of all analogs investigated in comparison with natural pheromone components of the turnip moth. The data also show that the grade of decrease of receptor interaction depends on specific structural changes within the molecule. The results demonstrate high complementary pheromone-receptor relationships, predominantly depending on the position of the unsaturated group in the chain, whereas analogs with other structural changes are still recognized as a pheromone-like compound by the receptor.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Brassica (protein targeting) ; Oil body ; Oleosin (in-vitro translation) ; Protein targeting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Oleosins of Brassica napus L. (oilseed rape) synthesized by in-vitro translation were found to be very efficiently targeted to microsomal membranes but only poorly translocated to oil bodies or emulsified oil. The use of other bilayer membranes as controls showed that this interaction was specific. The rate of oleosin synthesis in the presence of microsomes was enhanced about threefold, indicative of the involvement of the signal-recognition particle in the targeting process. There is no evidence for the cleavage of the protein during targeting and the protein sequence reveals no consensus cleavage site for the signal peptide. Protection experiments using Proteinase K revealed that about 6 kDa of the protein is exposed on the cytoplasmic side of the ER but the remainder is protected. Carbonate (pH 11) washing of microsomal membranes after in-vitro translation confirmed that oleosins have a domain which remains inserted in the ER rather than the protein being transported completely into the lumen of the ER. These results indicate that oleosins are transported via the ER prior to their accumulation on oil bodies.
    Type of Medium: Electronic Resource
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