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  • 1
    Electronic Resource
    Electronic Resource
    γ-Aminobutyric Acid Concentration in Cerebrospinal Fluid in Schizophrenia (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: γ-Aminobutyric acid (GABA) concentration was determined in cerebrospinal fluid (CSF) of acute and chronic schizophrenic patients, in persons with psycho-organic or personality disorders, and in nonpsychiatric controls. The mean CSF GABA level in the chronic schizophrenic patients was found to be significantly higher than in any of the other groups. No other statistically significant differences were found. Statistical analysis revealed that the elevated CSF GABA concentration in the chronic schizophrenic patients was unlikely to be caused by medication. These results are interpreted as evidence for possible primary or secondary GABAergic overactivity in the brain in chronic schizophrenia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb00579.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    ENZYMATIC N-METHYLATION OF INDOLEAMINES BY MAMMALIAN BRAIN: FACT OR ARTEFACT? (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Indoleamine-N-methyltransferase (INMT) activity in brain and other tissues from various species was investigated. Using conventional radiochemical assay techniques it was found that apparent INMT activity in brain was linear with time and concentration of protein, indoleamine substrate and methyl donor (S-adenosylmethionine). However, examination of the reaction products by means of exhaustive thin-layer chromatographic analysis failed to reveal evidence of significant N-methylation of tryptamine or N-methyltryptamine by S-adenosylmethionine. By contrast, with other tissues, notably rabbit lung. N-methylation of indoleamine was reproducibly demonstrable. The significance of these findings with reference to the transmethylation hypothesis of schizophrenia is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb10397.x
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of protein phosphorylation in acetylcholine receptor-enriched membrane preparations from torpedo fuscomaculata (1982)
    Springer
    Molecular and cellular biochemistry 42 (1982), S. 161-166 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary When the acetylcholine receptor (AChR*) from Torpedo is phosphorylated, ATP is found to bind non-covalently to the preparation. After correction is made for this binding of ATP, the phosphorylation reaction has a Km of 0,16 mM, a pH optimum of 8,6 and reaches maximal activity within 3 min. The intrinsic kinase activity is very specific for the AChR and does not phosphorylate either histones or phosvitin. The only amino acid to be phosphorylated is serine and cyclic GMP causes stimulation of the reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00238510
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  • 4
    Electronic Resource
    Electronic Resource
    Phosphorylation increases α-bungarotoxin binding to acetylcholine receptor-enriched membrane preparations (1983)
    Springer
    Molecular and cellular biochemistry 56 (1983), S. 67-71 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Acetylcholine receptor (AChR)-enriched membrane preparations from Torpedo electroplax bind α-bungarotoxin with a KD of 8.4 nM and the concentration of binding sites is 16 pmoles/mg protein. When, however, the α-toxin is incubated with receptor samples, phosphorylated in the presence of Mn2+ (10 mM) and ATP (0.5 mM), the concentration of binding sites is increased to 94 pmoles/mg protein, although there is no marked change in the KD (11 nM). Binding of acetylcholine to AChR-enriched membrane preparations occurs at a receptor which has two different conformational states with KD's of 8.4 nM and 520 nM. The concentration of binding sites for the high affinity component is l.35 pmoles/mg protein and for the low affinity component is 12 pmoles/ mg protein. The effect of phosphorylation of the AChR on agonist binding could not be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00228770
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  • 5
    Electronic Resource
    Electronic Resource
    Possible modulation of phosphorylation of acetylcholine receptor-enriched membrane preparations (1984)
    Springer
    Neurochemical research 9 (1984), S. 195-206 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract During phosphorylation of acetylcholine receptor (AChR)-enriched membrane preparations fromTorpedo fuscomaculata, phosphate is incorporated into a single protein, with a molecular weight corresponding to that of one of the receptor subunits (37,000 daltons). This protein also seems to contain the receptor binding site. ATP binds to four protein species, one of which corresponds to a different subunit of the receptor (molecular weight 45,000). Phosphorylation of these membrane preparations is affected by several factors, known to be involved in postsynaptic events. Ca2+ (10 μM) inhibits the reaction, whereas cGMP (20 μM), causes stimulation. Furthermore it has been shown that the agonists, acetylcholine, and carbamylcholine (10 μM and 1 μM) stimulate the phosphorylation reaction, while the antagonists, tubocurarine, hexamethonium, and decamethonium (1 μM), cause inhibition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964167
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