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  • Articles: DFG German National Licenses  (2)
  • 1970-1974  (2)
Source
  • Articles: DFG German National Licenses  (2)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 17 (1970), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —Levorphanol (10-3 M) reversibly blocked conduction in the giant axon of the squid and axons from the walking legs of spider crab and lobster. Similar concentrations of levallorphan and dextrorphan blocked conduction in the squid giant axon. Under the same experimental condition morphine caused an approximately 40 per cent decrease in spike height. Levorphanol did not affect the resting potential or resistance of the squid axon. Spermidine, spermine and dinitrophenol had little or no direct effect on the action potential nor did they alter the potency of levorphanol. Concentrations of levorphanol as low as 5 × 10-5 M blocked repetitive or spontaneous activity in the squid axon induced by decreasing the divalent cations in the medium. After exposure to tritiated levorphanol, the axoplasm and envelope of the squid axon accumulated up to 500 per cent of the concentration of tritium found in the external medium, dependent on time of exposure, and other variables. At pH 6 the levels of penetration were 33-50% of those found at pH 8, which correlates with our observation that levorphanol is about 33 % as potent in blocking the action potential at pH 6. The penetrability of levorphanol was not affected by spermidine, dinitrophenol or cottonmouth moccasin venom. Levorphanol did not alter the penetration of [C14]acetylcholine nor did it render the squid axon sensitive to it. The block of axonal conduction by compounds of the morphine series is discussed both as to possible mechanisms and significance.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Squid axonal preparations consisting of the giant axon plus adhering small nerve fibres were incubated for 30 min with phospholipase A (1, 0.2 and 0.025 mg/ml); phospholipase C (10 and 0.5 mg/ml) or lysolecithin (1 and 0.2 mg/ml) followed by another 30 min incubation in normal sea water. The axoplasm and envelope (sheath) of the axonal preparation were then separated and the phospholipids and free amino acids determined. The released amino acids were also measured in the incubation solutions. Compared to phospholipase C, phospholipase A caused a much greater reduction in the free amino acid content of axoplasm and envelope; and a concomitant much greater increase in amino acids released into the incubation solutions, even when phospholipase A was used in concentrations which caused less phospholipid splitting than phospholipase C. Lysolecithin had a much weaker effect than phospholipase A. It is concluded that disruption of hydrophobic binding has a much greater effect on the structure of the non-lipid portion of the axonal membranes than does disruption of hydrophilic (electrostatic) forces of interaction. Our results can be interpreted in terms of the protein-crystal or mosaic models of membrane structure whereas they do not support the unit membrane hypothesis.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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