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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 48 (1987), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Antibodies to Gm1 ganglioside enhance the release of γ-aminobutyric acid (GABA) from rat brain slices induced by depolarization with either 40 mM K+ or 200 μM veratrine. Three new observations are now reported, (a) GABA release induced by the Ca2+ ionophore A23187 was not affected by these antibodies. Because this Ca2+ ionophore causes transmitter release by bypassing depolarization-induced opening of Ca2+ channels, this result suggests that gangliosides participate either in the functioning of such Ca2+ channels or in the Na+ channels involved in depolarization, (b) The enhancement (by antibodies to GM1 ganglioside) of GABA release induced by high K+ levels occurred in the presence of tetrodotoxin (0.01 μM). (c) GABA release induced by veratrine in the absence of Ca2+ was not affected by the antibodies. These latter two observations indicate that Na+ channels are not involved in the action of the antibodies. We conclude that this evidence points to the participation of gangliosides in Ca2+ channel functions involved in GABA release in rat brain slices.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 68 (1946), S. 1671-1672 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 69 (1947), S. 2561-2563 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 68 (1946), S. 2697-2703 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 68 (1946), S. 2704-2705 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The subcellular distribution in rat brain cortex of six synaptic membrane antigens (56K, 58K, 62K, 63K, 64K, 66K) was studied by rocket immunoelectrophoresis, using antiserum to a highly purified synaptic plasma membrane fraction. Initial analysis of the insoluble portion of subcellular fractions showed that these antigens were also present in smooth microsomes, rough microsomes, and synaptic vesicles; that only traces were present in synaptic junctions; and that none was present in nuclei, mitochondria, and myelin. A trace amount of activity was also present in synaptic vesicle cytosol, but none in whole brain cytosol. Quantitative measurements of synaptic plasma membranes, smooth microsomes, and synaptic vesicles showed that all six antigens were present in synaptic plasma membranes and smooth microsomes, but that the 66K antigen was absent from synaptic vesicles. The 56K, 58K, 62K, 63K, and 64K antigens were present in highest concentration in synaptic plasma membranes, whereas the 66K antigen content was highest in smooth microsomes. Only the 58K, 62K, and 63K antigens were detectable in the membrane fraction of whole brain. Their enrichments in synaptic plasma membranes were 10.9, 5.4, and 5.9, respectively. We conclude that the 56K, 58K, 62K, 63K and 64K antigens are primary components of synaptic plasma membranes. The presence of synaptic plasma membrane antigens in smooth microsomes and synaptic vesicles probably represents material being actively transported, consistent with the hypothesis that proteins of synaptic plasma membranes and synaptic vesicles are transported via smooth endoplasmic reticulum.
    Type of Medium: Electronic Resource
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  • 7
    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 formation of a complex between myelin basic protein and S-100 protein was detected from the change in migration of S-100 protein on immunoelectrophoresis. A degree of specificity for the interaction was shown by two observations: (1) two other pure acidic proteins. III-III-2 and bovine serum albumin, did not show it and (2) complex formation was dependent on specific ions, either Ca2+ (10 mM) or Mn2+ (1 mM). Mg2+, Ba2+, and Li+ had no effect. Non-specific interactions between S-100 protein and other basic molecules (histones. polylysine) are not dependent on specific ions such as Ca2+ and Mn2+. The complex was stable at physiological salt concentrations and contained 3 mol of basic protein per mol of S-100 protein. Complex formation was also detected from the alteration of migration rate of S-100 protein in polyacrylamide gels. Serological activity (complement-fixation) of S-100 protein with anti-S-100 serum was reduced in the complex by 30%.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Rates of flow of glucose carbon in vivo into brain cholesterol, phospholipids, cerebrosides and gangliosides and concentrations of these lipids in the brain, were determined in adult rats after various periods of food deprivation. The rates were calculated from two measurements, the curve representing the decrease of plasma [14C]glucose specific activity with time and the specific activity of the brain lipid 180 min after intravenous injection of a tracer dose of d-[U-14C]glucose. Specific activities of brain lipids in rats deprived of food for 72h were significantly higher than in postabsorptive rats which were treated with the same dose of [14C]glucose. These higher specific activities were interpreted as a result of more labelled glucose available to lipid synthesis in the brain of fasted rats due to the substantial decrease in the rate of irreversible disposal of glucose by the whole body, commonly observed in fasted animals. The possibility that the higher specific activity values resulted from enhanced synthesis of brain lipids from glucose was ruled out since no changes were observed in the rate of flow of glucose carbon into brain lipids after food deprivation. The rate of flow of glucose carbon into gangliosides (15.4 ng C/min/mg C) was more than twice as fast as into either phospholipids or cerebrosides and about 4 times as fast as into cholesterol. The rates of carbon flow were used to calculate half lives of glucose carbon in the different classes of brain lipids. These half life values were 31 days for gangliosides, 72 days for phospholipids, 82 days for cerebrosides and 133 days for cholesterol. The results suggest that the synthesis of brain lipids from glucose is not affected by prolonged starvation in the adult rat.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A number of lipids known to be constituents of nerve-ending membranes were tested for their ability to inactivate botulinum toxin. Inactivation of the toxin by a lipid was taken as presumptive evidence that the lipid might be the in vivo receptor for the toxin. Several sphingolipids (sphingosine, galactosylceramide, glucosylceramide, lactosylceramide, cytolipin K and cytolipin R), steroids (cholesterol and deoxycholic acid) and fatty acids (palmitic acid, stearic acid, prostaglandin E1) did not affect the potency of botulinum toxin, and thus were discounted as potential toxin receptors. However, the gangliosides did inactivate botulinum toxin rapidly (in less than 5 min), within a temperature range of 2°-40°C, and at ionic strengths of 0.05-0.40. Inactivation diminished as pH fell below 6. The activity of gangliosides in suppressing the potency of botulinum toxin was a function of the number of sialic acid residues in the lipid. Thus, the data suggest that a molecule containing sialic acid may be the receptor for the toxin.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The conversion of plasma glucose into brain proteins in vivo was measured in rats after various periods of food deprivation. Rates of flow of glucose carbon into both soluble and insoluble brain proteins were calculated from the curve representing the decrease of plasma [14C]-glucose specific activity with time, and from the specific activity of brain protein 180 min after intravenous injection of a tracer dose of d-[14C]-glucose. Compared to the post-absorptive rats, food deprivation for 72 h caused a 30 per cent reduction in the rate of flow of glucose carbon into soluble brain proteins but did not affect the flow into insoluble proteins. Results of experiments in which the soluble brain proteins were separated by isoelectric focusing suggest that prolonged fasting in adult rats causes substantial differences in the conversion of glucose to different proteins.
    Type of Medium: Electronic Resource
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