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  • 1
    Electronic Resource
    Electronic Resource
    Inhibition by tetanus and botulinum A toxin of the release of [3H]noradrenaline and [3H]GABA from rat brain homogenate (1988)
    Springer
    Cellular and molecular life sciences 44 (1988), S. 224-226 
    Details
    ISSN: 1420-9071
    Keywords: Tetanus toxin ; botulinum toxin ; noradrenaline ; GABA ; brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rat brain homogenate was preloaded with [3H]noradrenaline or [3H]GABA and stimulated with high K+. Tetanus toxin and botulinum A neurotoxin partially prevent the evoked [3H]noradrenaline release in the same range of toxin concentrations starting below 10−10M. In contrast, release of γ-amino butyric acid (GABA) is much more sensitive to tetanus than to botulinum A toxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01941714
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  • 2
    Electronic Resource
    Electronic Resource
    Erwiderung (1989)
    Springer
    Journal of molecular medicine 67 (1989), S. 742-742 
    Details
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01721297
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  • 3
    Electronic Resource
    Electronic Resource
    Enzymatic hydrolysis of tetanus toxin by intrinsic and extrinsic proteases. Characterization of the fragments by monoclonal antibodies (1985)
    Springer
    Medical microbiology and immunology 174 (1985), S. 139-150 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Enzymatic fragments of tetanus toxin were characterized by immunoblotting using a set of previously characterized antibodies (Ahnert-Hilger et al. (1983) and a set of novel antibodies. The selected antibodis recognized the light chain, fragment C (Β 1), and the complementary piece (Β 2) of the heavy chain when blotted on nitrocellulose. All toxin preparations contained intrinsic esteroprotease activity which became manifest in the presence of urea. The main split product was a fragment (MW 100 000) reacting with anti-fragment C and anti-Β 2 antibodies. Toxicity does not depend on this protease activity. Some crude preparations of tetanus toxin contain another split product (MW 47 000) which resembles fragment C. The main product of papain hydrolysis is fragmentC, which appears as a double band under nonreducing conditions but is homogeneous when reduced. Chymotryptic digestion hydrolyses the heavy chain well but leaves the light chain largely intact. Tetanus toxin is very resistant against trypsin as compared with other proteases, although this enzyme splits numerous different links. Our data show the usefulness of immunoblotting with monoclonal antibodies in analytical work with tetanus toxin, and the relevance of intrinsic proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02298124
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  • 4
    Electronic Resource
    Electronic Resource
    Botulinum C2 toxin ADP-ribosylates actin (1986)
    [s.l.] : Nature Publishing Group
    Nature 322 (1986), S. 390-392 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Botulinum C2 toxin is a binary toxin and consists of two components, C2-I and C2-II, with relative molecular masses (Mrs) of 50K and 100K, respectively4. Both components are actually completely separate proteins which interact to cause the toxic effects. The 50K component, which is non-toxic in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/322390a0
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  • 5
    Electronic Resource
    Electronic Resource
    Oxoferin® und Natriumchlorit — Ein Vergleich (1989)
    Springer
    Journal of molecular medicine 67 (1989), S. 20-25 
    Details
    ISSN: 1432-1440
    Keywords: Oxoferin® ; Sodium chlorite ; Methaemoglobin ; Fibroblast ; Oxidant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Oxoferin®, a preparation approved for wound treatment, has been subjected to an in vitro analysis. 1. Oxoferin® produces methaemoglobin even if diluted 500fold, and leads to additional alterations if added in high concentrations to red cells. Sodium chlorite (NaClO2, 15 mM) is equivalent to undiluted Oxoferin®. 2. Oxoferin® in fiftyfold dilution damages fibroblasts in cell culture slowly and persistently. This dilution is equieffective with a 200 µM solution of sodium chlorite. Oxoferin® and sodium chlorite also damage vascular endothelial cells. 3. The oxidation equivalent of Oxyoferin® is 12.3 mM sodium chlorite. Our data indicate that Oxoferin® may be equated essentially with aqueous sodium chlorite.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01736530
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  • 6
    Electronic Resource
    Electronic Resource
    Depolarization increases inositolphosphate production in a particulate preparation from rat brain (1986)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 334 (1986), S. 1-9 
    Details
    ISSN: 1432-1912
    Keywords: Depolarization ; Ion channels ; Phosphatidylinositol ; Inositol phosphates ; Voltage-dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the accumulation of inositol phosphates (InsP) due to depolarization. A particulate preparation of rat brain was introduced to rule out transmitter activated mechanisms and to allow free access for drugs of high molecular weights. Potassium depolarization doubled InsP within a few minutes. InsP accumulation depended on time and K+ concentration, and was affected neither by tetrodotoxin nor by atropine. Radioactive metabolites co-eluted with inositol mono-phosphate and inositol bis-phosphate, whereas only minor amounts appeared with inositol tris-phosphate. The content in phosphatidylinositols was decreased. No evidence was found for the involvement of a neurotransmitter. Sea anemone toxin II (around 1 μmol/l), which keeps the Na+-channels open, promoted the InsP accumulation in an atropine-resistant manner. Tetrodotoxin prevented it when given before, and inhibited it when given after initiation by sea anemone toxin II. Moreover the K+ channel blockers 4-aminopyridine, dendrotoxin and tetraethylammonium all caused InsP accumulation. Palytoxin was by far the most potent promoter of InsP accumulation with a detection limit below 10 pmol/l, and displayed a unique bell-shaped concentration-effect correlation. Ouabain (3 μmol/l) and above) also elicited the InsP accumulation. The response to carbachol was not only inhibited completely by atropine, but also partially (more than 50%) by tetrodotoxin, which indicates the involvement of voltage-dependent sodium channels in the receptor-triggered InsP accumulation. Thus independent of the causative agent, depolarization promotes an InsP accumulation. We conclude that degradation of phosphatidylinositols is mediated not only by receptor occupation but also by a positive shift in membrane voltage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498733
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  • 7
    Electronic Resource
    Electronic Resource
    Electrophysiological and neurobiochemical evidence for the blockade of a potassium channel by dendrotoxin (1985)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 330 (1985), S. 77-83 
    Details
    ISSN: 1432-1912
    Keywords: Dendrotoxin ; Potassium channel ; Nerve fibre ; Depolarization ; GABA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of dendrotoxin (DTX), a toxic peptide from Dendroaspis angusticeps venom, were studied electrophysiologically on peripheral frog nerve fibres, and biochemically on large synaptosomes from rat brain. 1. On nerve fibres, DTX reduced the amplitude and prolonged the duration of the action potential; even at 0.1 nmol/l DTX produced significant effects. Maximum block of potassium currents occurred at about 30 nmol/l. Turning on of the remaining current was slowed. Reversibility was incomplete. The reduction of potassium currents was between 31% and 85% at 85 nmol/l DTX (n=8). The remainder appeared to be resistant to DTX. Sodium channels were not affected. 2. On large synaptosomes DTX (above 1 nmol/l) produced a slight depolarization, indicated by an outward shift of the lipophilic cation tetraphenylphosphonium, and promoted the release of radioactivity after preloading with [3H] GABA. DTX had similar potency but lower efficacy in this respect than sea anemone toxin II (ATX II). In contrast to the effects of ATX II, those due to DTX were only partially inhibited by tetrodotoxin. The actions of 4-aminopyridine resembled those of DTX, but the latter was about 500 times more potent. The electrophysiological data provide direct evidence for blockade of a potassium channel by DTX. This action is sufficient to explain the biochemical observations, although additional effects on synaptosomes cannot be excluded.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499898
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