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  • 1975-1979  (4)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of medicinal chemistry 18 (1975), S. 29-33 
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Nicotine binds to homogenates of lobster walking leg nerve (Kd= 1.1 ± 0.3 μm, Bmax= 2.4 ± 0.5 nmol/g wet tissue), horseshoe crab leg nerve (Kd= 0.11 ± 0.06 μm, Bmax= 1.3 ± 0.6nmol/g), and kidney from 18-month-old rats (Kd= 0.8 ± 0.2 μm, Bmax= 23 ± 9 nmol/g). The pharmacological sensitivities of nicotine binding to lobster and horseshoe crab leg nerve homogenates are similar to that of the axonal cholinergic binding macromolecule (ACBM) (Denburget al., 1972) of lobster leg. nerve membrane, while the binding to rat kidney is sensitive to α-bungarotoxin but not atropine or curare. There was no nicotine binding to rat heart or spleen, or to kidney from younger rats; little or no binding to blue crab nerve or to Torpedo electroplax motor nerve; and little binding (around 0.1 nmol/g) to rat liver. [3H]α-Bungarotoxin bound reversibly (0.17 nmol/g) to lobster leg nerve membrane The implications of these results for the distribution and function of the ACBM, and for the specificity of α-bungarotoxin, are discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The in vitro uptake of exogenous acetylcholine by isolated presynaptic vesicles has been demonstrated in a new system. A preparation of vesicles from Torpedo californica electroplax was developed in which acetylcholinesterase and acetylcholine receptor activity were blocked. The vesicles bound acetylcholine with Kd 1.58 μM, the maximum amount bound being 26 pmol per g of original tissue, or 52 molecules per vesicle. Nicotinic drugs blocked binding, but muscarinic and noncholinergic drugs did not. The relative potency of nicotinic drugs differed greatly from their potency on Torpedo receptor. Sephadex chromatography showed that 26% of the binding was irreversible. The relationship of the binding to acetylcholine uptake and storage was discussed.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 23 (1975), S. 91-101 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The basis for the ability of α-dihydrograyanotoxin II (α-2HG-II) to promote Na+ conductance in axons was sought. The apparent binding of tritiated α-2HG-II to neural and other preparations was studied, using equilibrium dialysis, with lobster axon membranes,Torpedo electroplax, housefly head, and rat brain, liver and kidney. In every case the “binding” was nonsaturating and was suggested to involve nonspecific partitioning into the tissue. Supporting evidence was the similarity of extent of “binding” in all tissues and its relative insensitivity to neuropharmacological agents. α-2HG-II did not affect the Na+ conductance of phospholipid bilayers, nor did it permit transport of22Na into a bulk organic phase. It was concluded that α-2HG-II did not bind to the sodium gate, but possibly to a sodium permease present at a frequency of less than one perμ 2 of cell membrane.
    Type of Medium: Electronic Resource
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