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  • 1
    Electronic Resource
    Electronic Resource
    LABTRAN. Language and system for programming chemical experiments (1972)
    s.l. : American Chemical Society
    Analytical chemistry 44 (1972), S. 339-343 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60310a003
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  • 2
    Electronic Resource
    Electronic Resource
    Residues of mirex in channel catfish and other aquatic organisms (1973)
    Springer
    Bulletin of environmental contamination and toxicology 10 (1973), S. 73-77 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01685875
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  • 3
    Electronic Resource
    Electronic Resource
    Lithium (1971)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Pharmacology 11 (1971), S. 285-302 
    Details
    ISSN: 0362-1642
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pa.11.040171.001441
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  • 4
    Electronic Resource
    Electronic Resource
    Applications of Fourier transform techniques to steric-exclusion Chromatography (1974)
    s.l. : American Chemical Society
    Analytical chemistry 46 (1974), S. 637-642 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60342a019
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  • 5
    Electronic Resource
    Electronic Resource
    Instability of current followers in potentiostat circuits (1974)
    s.l. : American Chemical Society
    Analytical chemistry 46 (1974), S. 647-650 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60342a006
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  • 6
    Electronic Resource
    Electronic Resource
    METAL CHELATES IN THE STORAGE AND TRANSPORT OF NEUROTRANSMITTERS: INTERACTIONS OF Cu2+ WITH ATP AND BIOGENIC AMINES (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The thermodynamic stabilities of the coordinate binding of Cu2+ ion with adenosinetriphos-phate (ATP) and several biogenic amines have been determined in aqueous model systems in an attempt to examine the possible correlation between metal-amine binding and the in vivo affinities of the amines for granule-binding. In each of the ternary chelate systems consisting of Cu2+-ATP-amine (1:1:1), the Cu2+ ion is preferentially bound by ATP in the pH range 3–5 with a stability constant of Log KML= 517. In the pH range 5–8 each of the biogenic amines coordinates with Cu2+ -ATP chelate to form the respective ternary chelate. The nature and strength of binding of fourteen different amines with Cu2+-ATP have been evaluated on the basis of the stabilities of the ternary chelates. On the basis of the quantitative equilibrium data generated in this study, it appears that both pyrocatechol moiety and the ethanolamine side-chain of the catechol amines are involved in the coordination of copper. The metal-binding stabilities of the biogenic amines are then correlated with the molecular structure, donor basicities and the in vivo affinities of the amines for granule-binding in order to rationalize the possible involvement of metal chelates in the monoamine binding, storage and transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb12190.x
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  • 7
    Electronic Resource
    Electronic Resource
    THE EFFECT OF HYPOXIA ON MONOAMINE SYNTHESIS, LEVELS AND METABOLISM IN RAT BRAIN (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Rats were exposed to 5.6% oxygen environments for up to 2 h. The accumulation of brain DOPA and 5-hydroxytryptophan at 30 min after decarboxylase inhibition was used to estimate cerebral tryosine and tryptophan hydroxylase activity, respectively, in vivo. There was a continuing decrease in tryosine hydroxylase activity during the 2 h in whole brain as well as five brain regions. Tryptophan hydroxylase activity declined during the 1st h, but then increased towards control levels during the 2nd h. There was an increase in brain tryptophan during the 2nd h as well. In whole brain and the five brain regions, there was no significant change in the levels of noradrenaline, dopamine or 5-hydroxytrypamine. During a 1 h exposure to 5.6% oxygen, there was decreased accumulation of noradrenaline, dopamine and 5-hydroxytryptamine after MAO inhibition and decreased accumulation of homovanillic acid and 5-hydroxyindoleacetic acid after probenecid administration. The dercreased synthesis and metabolism of the monoamines is most likely attributable to insufficient brain tissue oxygen as a substrate for the two hydroxylase enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb07522.x
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  • 8
    Electronic Resource
    Electronic Resource
    METAL CHELATES IN THE STORAGE AND TRANSPORT OF NEUROTRANSMITTERS: FORMATION OF MIXED LIGAND CHELATES OF Mg2+-ATP WITH BIOGENIC AMINES (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Quantitative studies on the interactions of adenosine-triphosphate and several biogenic amines with magnesium ion have been carried out in an attempt to correlate the thermodynamic stabilities of the metal-binding of the amines with the in vivo affinities of the amines for granule-binding. Equilibrium data indicate that in each of the ternary chelate systems (viz. Mg2+-ATP-amine), the predominant reaction in the pH range 3.0–7.0 is the formation of a magnesium-ATP chelate with a stability constant, log KML=3.22 ± 0.02. Each of the biogenic amines coordinates with Mg2+-ATP system in the pH range 7.0–10.5 to form the mixed ligand chelate (or ternary chelate), Mg2+-ATP-amine(1:1:1). The stability constants for the binding of the amines with Mg2+-ATP are: (i) norepinephrine (NE) = 2.34 ± 0.32; (ii) epinephrine (E) = 2.95 ± 0.08; (iii) dopamine (DA) = 3.05 ± 0.06; (iv) octopamine (OA) = 1.93 ± 0.12; (v) 6-hydroxydopamine (6-HDA) = 2.42 ± 0.14; (vi) 3-methoxynorephedrine (MeN) =2.76 ± 0.09; (vii) amphetamine (AA) =2.09 ± 0.05; (viii) tyramine (TA) = 2.60 ± 0.04; (ix) phenylethylamine (PEA) = 0.A general correlation is indicated between the stability constants (binding strengths) of the amine chelates and the metal-binding functionalities of the amines on the one hand and their vesicular binding characteristics in in vivo systems on the other (Carlsson and Waldeck, 1966). The Mg2+-ATP-dependant amine storage mechanism of KIRSHNER (1962a;b) and Carlsson, Hillårp and Waldeck (1963) is discussed both in the light of the data on metal chelate stability and of a significant modification of metal coordination hypothesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01430.x
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of hypoxia on tyrosine and tryptophan hydroxylation in unanaesthetized rat brain (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The Tyrosine and tryptophan hydroxylase enzymes have been proposed as rate-limiting steps in the biosynthesis of catecholamines and 5-hydroxytryptamine (5-HT), respectively; thus under normal physiological conditions the rate of amine synthesis appears to be controlled by the activity of these hydroxylase enzymes (see Udenfriend, 1966; Lovenberg, Jequier and Sjoerdsma, 1968). Subtle changes in neuronal activity may result not in changes in the levels of the amine neurotransmitters, but rather in alteration in their production and metabolism without measurable change in their levels. Previous studies of the effect of hypoxia on monoamines have dealt with amine levels, but there have been no studies of the effect of lowered oxygen on the synthesis of these substances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00055.x
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  • 10
    Electronic Resource
    Electronic Resource
    METAL CHELATES IN THE STORAGE AND TRANSPORT OF NEUROTRANSMITTERS: INTERACTIONS OF METAL IONS WITH BIOGENIC AMINES (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Equilibrium studies on the interaction of biogenic amines with iron (Fe2+ and Fe3+) and magnesium (Mg2+) were undertaken in an attempt to correlate the stabilities of metal-amine chelates and the reported granule-binding affinities of the biogenic amines. By means of potentiometric equilibrium measurements at 25°C and an ionic strength of 10 (KNO3) the formation constants of the Fe2+ chelates with norepinephrine (NE) and adenosine-S-triphosphate (ATP) were determined. Possible structures were derived for the co-ordinate binding of Fe2 + with NE. The interactions of Fe2+ and Fe2+-ATP with NE were investigated and the formation of Fe2+-NE-ATP (1:1:1) mixed ligand ternary chelate was proposed on the basis of the equilibrium data. Information obtained from chelation studies of Fe2+ with pyrocatechol and ethanolamine taken together with the data obtained on the Fe2+-NE system indicated that the binding of Fe2+ by NE was probably via the pyrocatechol moiety. Equilibrium constants for the binding of tyramine (TA) dopamine (DA) and NE with Mg2+ were also determined. The equilibrium data obtained on the Mg2+-amine systems indicated a correlation between the metal-amine binding affinities and the structure and amine-release (and storage) activities of the biogenic amines. A consideration of the stabilities of the Fe2+ and Mg2+ chelates together with the occurrence of these metal ions in synaptosomes suggests their possible involvement in the intra vesicular amine-binding and storage sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb11963.x
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