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  • Chaperone  (1)
  • Chemoreception  (1)
  • General Chemistry
  • Condensed Matter: Electronic Properties, etc.
  • 1995-1999  (2)
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Keywords
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Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Processing of antennular input in the brain of the spiny lobster, Panulirus argus (1996)
    Springer
    Journal of comparative physiology 178 (1996), S. 579-604 
    Details
    ISSN: 1432-1351
    Keywords: Crustacean ; Chemoreception ; Mechanoreception ; Deutocerebrum ; Motoneurons ; Projection neurons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Neurons in the brain of the spiny lobster that respond to chemical and mechanical stimulation of the antennule (antenna I) were recorded and stained intracellularly. Described here are neurons that do not arborize in the olfactory and accessory lobes of the deutocerebrum, but rather primarily target the lateral and/or the median antennular neuropils of the deutocerebrum. Some of the neurons also extend into the antennal and tegumentary neuropils of the tritocerebrum and the neuropils of the median protocerebrum. Included are antennular sensory afferents, antennular motoneurons, projection neurons descending from the central brain, projection neurons ascending from the central brain and projection neurons descending from the eyestalk ganglia. Collectively, these neurons consitutute a novel antennular sensory pathway that is parallel to and independent of the antennular olfactory pathway. The novel pathway integrates mechanosensory and non-olfactory chemosensory information in the lateral and/or the median antennular neuropils, which also serve as lower motor centers of the antennule. Division of the arthropod deutocerebrum into two, functionally distinct chemosensory pathways may reflect differences in how chemosensory information is processed that is fundamental to understanding the origin of the sense of smell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227374
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions (1996)
    Springer
    Planta 200 (1996), S. 326-334 
    Details
    ISSN: 1432-2048
    Keywords: Chaperone ; Chloroplasts ; Chromoplasts ; Heat-shock protein ; Secale
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A partial cDNA which codes for the β-subunit of a plastidic chaperonin 60 (cpn60-β) from rye (Secale cereale L.) leaves was identified and sequenced, except for 46 amino acids of the N-terminus of the mature protein and the transit sequence. This is the first cpn60-β sequence determined for a monocotyledonous plant. Specific antibodies against cpn60-β were affinity-purified from an antiserum raised against the total soluble protein fraction of ribosome-deficient plastids. The localization of cpn60-β in chloroplasts or non-green plastids was confirmed by immunodetection in Percoll gradient-purified organelles. The expression and occurrence of cpn60-β was analysed by immunoblotting with the specific antibodies and Northern hybridization. The cpn60-β protein was constitutively expressed in various green and non-green tissues. It was evenly distributed along the major part of a rye leaf, while highest transcript levels occurred in the youngest and oldest leaf sections. The expression of the cpn60-β protein was not enhanced by a heat-shock treatment at 42 °C. The cpn60-β transcript and protein were more strongly expressed in various non-green, for instance etiolated, 70S-ribosome-deficient 32 °C-grown, or herbicide-bleached tissues, than in green leaves of rye. A rapid increase in the cpn60-β transcript level was also observed when green leaves were transferred from light to darkness while the protein level was not affected. The dark-induced increase in the cpn60-β transcript was totally suppressed in the presence of 2% sucrose. Inhibitor treatments suggested that the change in cpn60-β transcript level was not related to changes of the ATP supply of the tissue. While the large subunit of the photosynthetic protein ribulose-1,5-bisphosphate carboxylase was largely degraded during ripening of tomato fruits, high levels of cpn60-β were detected in tomato chromoplasts and in the yellow flower petals of Narcissus. Low levels of cpn60-β were detected in root tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00200300
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    Paper (German National Licenses)
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