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  • 1975-1979  (36)
  • 1970-1974  (24)
  • 1935-1939  (15)
  • 1920-1924  (3)
  • 1905-1909  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Optimization of the coupled enzymic measurement of substrate (1979)
    s.l. : American Chemical Society
    Analytical chemistry 51 (1979), S. 529-533 
    Details
    ISSN: 1520-6882
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ac50040a018
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  • 2
    Digitale Medien
    Digitale Medien
    Optimized wide-interval rate measurements of substrate (1979)
    s.l. : American Chemical Society
    Analytical chemistry 51 (1979), S. 526-528 
    Details
    ISSN: 1520-6882
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ac50040a017
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  • 3
    Digitale Medien
    Digitale Medien
    ATTEMPTS TO PREPARE GREEN GOLD SOLS1 (1938)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 42 (1938), S. 1149-1150 
    Details
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/j100903a501
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  • 4
    Digitale Medien
    Digitale Medien
    Synthesis in the 1,2,3,4-Tetrahydroquinoline Series (1939)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 61 (1939), S. 2830-2832 
    Details
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ja01265a078
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  • 5
    Digitale Medien
    Digitale Medien
    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
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ac60310a003
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  • 6
    Digitale Medien
    Digitale Medien
    SYNAPTOSOMAL TYROSINE HYDROXYLATION: AFFINITY FOR OXYGEN (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract— Crude striatal synaptosomes were used to determine the affinity of brain tyrosine 3-mono oxygenase for oxygen. The rate of tyrosine hydroxylation was determined at several different oxygen concentrations using L-[14C]tyrosine as substrate and measuring the [14C]DOPA formed in the presence of a decarboxylase inhibitor. The accumulation of [14C]tyrosine by synaptosomes was unaffected by incubation in nitrogen or 2.3% oxygen. Preincubation in nitrogen for up to 4 h did not impair the ability of synaptosomes to hydroxylate tyrosine when returned to air. Furthermore, pre-incubation in either nitrogen or air produced similar changes in the ultrastructural appearance of the synaptosomes and mitochondria in the crude preparation used in these studies. Thus tyrosine hydroxylation in these synaptosomes appeared to reflect tyrosine 3-mono oxygenase activity over a range of oxygen concentrations. The apparent Km for oxygen was 2 × 10−5 at pH 6.7 and 7.4. The apparent Km was not significantly altered by the addition of Ca2+, and was slightly increased in the presence of N6-mono-butyryl cyclic AMP or high K+. These data are consistent with the hypothesis that the availability of oxygen may limit catecholamine synthesis in the intact rat brain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10667.x
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  • 7
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01430.x
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  • 8
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb11963.x
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  • 9
    Digitale Medien
    Digitale Medien
    BRAIN TYROSINE HYDROXYLATION: ALTERATION OF OXYGEN AFFINITY IN VIVO BY IMMOBILIZATION OR ELECTROSHOCK IN THE RAT (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract— The rates of brain tyrosine and tryptophan hydroxylation, estimated in vivo from the accumulation of DOPA and 5-hydroxytryptophan after the administration of a decarboxylase inhibitor, appear dependent on the availability of oxygen as a substrate. During two types of physical stress, electroshock and curare-immobilization, the rate of brain tyrosine hydroxylation was greater than in unstressed controls and was not significantly decreased when the stresssed animals were made hypoxic. The loss of oxygen dependence by brain tyrosine hydroxylation during stress was observed in several brain regions and was not associated with alterations in the concentrations of brain tyrosine. tryptophan, serotonin, dopamine or norepinephrine. The rate of brain tryptophan hydroxylation was not affected by stress and remained oxygen dependent. The increase in catecholamine synthesis during stress appears to be the result of increased catecholaminergic nerve impulse flow. These experiments are consistent with the hypothesis that during neuronal stimulation an allosteric change in tyrosine hydroxylase increases the affinity of the enzyme for oxygen allowing greater catecholamine synthesis despite limiting concentrations of this substrate.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb01566.x
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  • 10
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00055.x
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