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  • 1
    ISSN: 1573-1561
    Keywords: Insecticide ; fumigant ; terpenoids ; Coleoptera ; Bruchidae ; Curculionidae ; camphor ; carvacrol ; Monarda fistulosa ; Artemisia tridentata ; Zabrotes subfasciatus ; Sitophilus oryzae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Leaves of two highly aromatic plants,Artemisia tridentata (Nutt.) andMonarda fistulosa L., prepared according to a patented process, inhibited oviposition by the Mexican bean weevil,Zabrotes subfasciatus (Boheman), in beans at concentrations less than 1% w/w. Both plant species were less effective against the rice weevil,Sitophilus oryzae L., in wheat, with onlyM. fistulosa exhibiting any concentration-dependent activity. The maximal control achieved against this species was less than 50% at 3% w/w. Two less aromatic plant species,Balsamorhiza sagittata (Pursh.) Nutt. andGeranium viscosissimum Fisch. and Mey., caused only low levels of inhibition against both insect species. Volatiles probably caused the response toA. tridentata andM. fistulosa, while the asymptotic concentration dependence for the less volatile plant material was likely caused by behavioral factors related to the physical presence of foreign particulate matter in the foodstuff. Chemical analysis indicated that most of the volatile components from the dried leaf material from all species were terpenoids, with camphor (9.7 mg/g) and 1,8-cineole (4.0 mg/g) being most abundant inA. tridentata and carvacrol (26.3 mg/g) being most abundant inM. fistulosa.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 26 (1993), S. 366-373 
    ISSN: 1059-910X
    Keywords: Immunogold labeling ; Electron microscopy ; Lung ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Surfactant proteins A, B, and C (SP-A, SP-B, and SP-C) are synthesized in alveolar type II cells. SP-B and SP-C are both synthesized as large precursor molecules that are proteolytically processed to their mature sizes. In a previous immunoelectron microscopic study, we showed that precursor SP-B is processed to its mature size in multivesicular bodies. In the present study, using a specific antibody aginst precursor SP-C, we demonstrate that precursor SP-C is present in the same intracellular compartments of the biosynthetic pathway, i.e., endoplasmic reticulum, Golgi complex, and multivesicular bodies, as precursor SP-B. Since mature SP-C is known to be present in multilamellar bodies, this suggests a biosynthetic routing and site of processing of this protein similar to those of SP-B. Double-labeling experiments using antibodies against SP-A, precursor SP-B, precursor SP-C, and an antibody against HA I, an adaptor protein involved in the budding of transport vesicles from the Golgi complex, showed that the different surfactant proteins traverse and exit the Golgi complex via the same route. The surfactant proteins do not exit the Golgi complex via HA I-positive coated buds or vesicles. These data are in accordance with the concept that SP-A, SP-B, and SP-C are transported together through the same biosynthetic pathway via multivesicular bodies to multilamellar bodies. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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