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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (88)
  • Wiley-Blackwell  (88)
  • American Geophysical Union
  • American Institute of Physics (AIP)
  • MDPI Publishing
  • Oxford University Press
  • 1990-1994  (88)
  • 1991  (88)
Collection
Publisher
  • Wiley-Blackwell  (88)
  • American Geophysical Union
  • American Institute of Physics (AIP)
  • MDPI Publishing
  • Oxford University Press
Years
  • 1990-1994  (88)
Year
  • 1
    ISSN: 0739-4462
    Keywords: ecdysteroids ; makisterone A ; 20-hydroxyecdysone ; enzyme immunoassay (EIA) ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The major ecdysteroids in large worker pupae of the leaf-cutting ant Acromyrmex octospinosus were characterized at the peak ecdysteroid concentration by using high-performance liquid chromatography, enzyme immunoassay, and mass spectrometry. In decreasing amounts, they were determined to be makisterone A, an unidentified C28 ecdysteroid bearing a molecular weight of 494, 20-hydroxyecdysone (ratio of 1 to 6 as compared to makisterone A), and putative but negligible ecdysone. The presence of both C28 and C27 ecdysteroids is discussed in relation to the content of 4-desmethylsterols determined by gas chromatography and mass spectrometry to be ergosta-5,7,24 (28)-trien-3β-ol, ergosterol, ergosta-5,7-dien-3β-ol and ergosta-7,24(28)-dien-3β-ol for the main sterols, and with a small amount of cholesterol.
    Additional Material: 4 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 69-79 
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 5 Tab.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 107-122 
    ISSN: 0739-4462
    Keywords: [3H]quinuclidinyl benzilate ; radio-ligand binding ; autoradiography ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of [3H]quinuclidinyl benzilate to a cockroach brain preparation was investigated. Specific binding was saturable with a Kd of 0.25 nM and Scatchard analysis indicated a Bmax of 604 pmol/mg protein. Kinetic analysis indicated that the ligand is binding in a complex fashion while dissociation followed a simple kinetic process. The pharmacology of the site was typical of muscarinic receptors but the site cannot be characterized in terms of vertebrate muscarinic-receptor subtypes. Affinity of the receptor for agonists was modulated by Mg2+ and guanylylimidodiphosphate but not by pertussis toxin indicating the involvement of a pertussis-toxin insensitive G-protein. Carbamylcholine did not inhibit basal or forskolin-stimulated adenylate cyclase activity. The binding site was localized autoradiographically and was restricted to the median and lateral calyces of the brain.
    Additional Material: 5 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 139-152 
    ISSN: 0739-4462
    Keywords: superoxide dismutase ; catalase ; glutathione peroxidase ; glutathione reductase ; hypericin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Many secondary plant compounds are capable of photoactivation resulting in the production of toxic species of oxygen. One mechanism of defense for insects feeding on phototoxic plants may be the presence of antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPOX), and glutathione reductase (GR). The activities of these enzymes were examined in larvae of three lepidoptera: Ostrinia nubilalis, Manduca sexta, and Anaitis plagiata. Highest levels of antioxidant enzyme activity were found in A. plagiata, a specialist feeder on Hypericum perforatum, which contains high levels of the phototoxin hypericin. Larvae of A. plagiata fed leaf discs treated with hypericin exhibited a short-term, concentration-dependent decline in enzyme activity. Longer term studies with A. palgiata fed either the photoxic H. perforatum, or the closely related but non-phototoxic H. calycinum, resulted in increased CAT and GR activity in larvae fed the phototoxic plant whereas SOD activity was not significantly different. These results suggest that CAT and GR may be inducible defenses against phototoxins.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 189-200 
    ISSN: 0739-4462
    Keywords: cultured insect cells ; Aedes albopictus ; transient expression ; hsp-cat plasmid ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trnsient expression of a heat-shock protein-chloramphenicol acteyltrans-Perase (hsp-CAT) recombinant plasmid was used to define the parameters that influence transfection of cultured mosquito cells using DNA-calcium phosphate coprecipitates. The efficiency of the calcium phosphate procedure was strongly influenced by the growth state of recipient cells, and by the temperature at which the coprecipitate was prepared. Under optimal conditions, which included formation of the DNA-calcium phosphate coprecipitate at 50°C, transfection frequencies were up to tenfold higher than those obtained using the previously described polybrene procedure.
    Additional Material: 4 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 215-215 
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 221-234 
    ISSN: 0739-4462
    Keywords: vitellogenesis ; hemolymph proteins ; transplanted ovaries ; follicle growth ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ovaries from Lymantria dispar females were transplanted into an environment lacking vitellogenin, the male milieu, in order to determine how the presence of vitellogenin in the hemolymph affects the process of protein uptake by gypsy moth oocytes. When undeveloped ovaries from newly ecdysed last instar females were transplanted into males of the same stage, follicles detached from the germarium and increased in size, but the growth of oocytes proceeded more slowly than those from female controls. Although chorion fromation was delayed in male-grown ovaries, scanning electron microscopy of chorionated eggs recovered from adult males showed that a chorion with normal surface architecture was formed by the adult stage. SDS-PAGE analysis of the male-grown ovaries and hemolymph from males receiving ovaries showed that vitellogenin production was not stimulated by the organ transplant and only male hemolymph proteins were internalized by the male-incubated ovaries. Thus, in the absence of vitellogenin, endocytosis of male hemolymph proteins occurred, but the rate of oocyte growth was slowed.
    Additional Material: 8 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991) 
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991), S. 201-211 
    ISSN: 0739-4462
    Keywords: plant phototoxins ; broad-spectrum biocides ; potential plant enemies ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Plant phototoxins are broad-spectrum biocides which adversely affect an array of potential plant enemies, including among others disease-causing pathogens, nematodes, insect herbivores, and competing plant species. Thus far, plants which contain these broad-spectrum allelochemicals have been found to occur in open habitats (i.e., in full sunlight) where a defensive mechanism mediated by light would seem to operate most effectively. The levels of available light in shaded environments, although considerably lower than full sun (1-10% of full sun), are equivalent to the intensities of light used to kill phototoxin-treated insects in laboratory studies. This suggests that phototoxic reactions might mediate important organismal interactions in shaded environments as well. In this study, more than 230 Costa Rican rainforest plants were bioassayed for phototoxic metabolites in an effort to ascertain their prevalence among plants growing in moderate to extreme shade. Microbial bioassays, employing Bacillus cereus (a gram positive bacterium), Escherichia coli (a gram negative bacterium), and Saccharomyces cerevisiae (a yeast) were used to rapidly and sensitively indicate phototoxic action and potential for insecticidal action. Tissue extracts from 12 plant families tested positive for phototoxins. This is the first report of phototoxins occurring in eight of those families (Acanthaceae, Campanulaceae, Gesnariaceae, Loganiaceae, Malpigaceae, Phytolaccaceae, Piperaceae, and Sapotaceae). The presence of phototoxins in rainforest plants suggests that phototoxic plant allelochemicals may function as important defenses in low-light, as well as high-light, environments.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991), S. 67-80 
    ISSN: 0739-4462
    Keywords: insect immunity ; lumen ; epithelium ; fifth larval stadium ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Low levels of lysozyme were found in the midgut epithelium of the tobacco hornworm, Manduca sexta, during the early part of the fifth larval stadium. This was observed in control insects as well as in bacterially challenged insects. No lysozyme was detected in the gut contents of either group of insects which were actively eating or in the early stages of metamorphosis. However, high levels of lysozyme activity were detected in homogenates of midgut tissue collected from insects later in the stadium. Immunocytochemical studies demonstrated that lysozyme accumulates in large apical vacuoles in regenerative cells of the midgut during the larval-pupal molt. These cells, initially scattered basally throughout the larval midgut epithelium, multiply and form a continuous cell layer underneath the larval midgut cells. At the larval/pupal ecdysis the larval midgut epithelium is sloughed off and the regenerative cells, now forming the single cell layer of the midgut, release the contents of their vacuoles into the midgut lumen. This release results in high lysozyme activity in the lumen of the pupal midgut and is thought to confer protection from bacterial infection. This is the first indication that the lysozyme gene may be developmentally regulated in a specific tissue in the absence of a bacterial infection.
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