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  • 1
    Electronic Resource
    Electronic Resource
    Particle-induced desorption mass spectrometry with a quadrupole mass spectrometer (1984)
    s.l. : American Chemical Society
    Analytical chemistry 56 (1984), S. 308-311 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00266a047
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  • 2
    Electronic Resource
    Electronic Resource
    Fused silica capillary gas chromatography/negative chemical ionization mass spectrometry for determination of catecholamines and their O-methylated metabolites (1982)
    s.l. : American Chemical Society
    Analytical chemistry 54 (1982), S. 1806-1811 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00248a034
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Serotonin and pituitary-adrenal function (1974)
    [s.l.] : Nature Publishing Group
    Nature 248 (1974), S. 424-426 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We used male Sprague-Dawley rats (150-200 g). They were kept in a 12L:12D environment (lights on at 0700 h) and given food and water ad libitum. Serum corticosterone was assayed fluorometrically, while the determination of serum ACTH was made by bioassay5. The concentrations of brain serotonin were ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/248424a0
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  • 4
    Electronic Resource
    Electronic Resource
    Stimulation of synaptosomal dopamine synthesis by veratridine (1974)
    [s.l.] : Nature Publishing Group
    Nature 250 (1974), S. 737-739 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Male Sprague-Dawley rats (200?250 g) were decapitated and the striatum was dissected out and placed in polyethylene tubes in ice. The P2 fraction (containing synaptosomes, mitochondria and myelin) was prepared essentially as described by Gray and Whitaker14. Most of the tyrosine hydroxylase ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/250737a0
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  • 5
    Electronic Resource
    Electronic Resource
    Enzymatic Synthesis of Adrenaline in Mammalian Brain (1969)
    [s.l.] : Nature Publishing Group
    Nature 221 (1969), S. 368-369 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Brain areas from adult Simonson rats were dissected and homogenized in equal volumes of ice-cold isotonic potassium chloride. The homogenates were centrifuged at 50,000g for 1 h, and the pellets resuspended in 10 volumes of isotonic KCl. Assay for adrenaline forming activity was carried out as ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/221368a0
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  • 6
    Electronic Resource
    Electronic Resource
    Measurement of Methionine-Enkephalin [Arg6,Phe7] in Rat Brain by Specific Radioimmunoassay Directed at Methionine Sulphoxide Enkephalin[Arg6,Phe7] (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A specific and sensitive radioimmunoassay procedure for Metenkephalin[Arg6,Phe7] which allows its measurement in regions of the rat brain is described. The antiserum was raised against the methionine sulphoxide derivative of the peptide, and all samples and standards were oxidized with hydrogen peroxide prior to use in the assay with chloramine T-oxidized 125I-labelled Met(O)-enkephalin[Arg6,Phe7]. The only significant cross-reactivity was 30% with the reduced heptapeptide Met-enkephalin[Arg6,Phe7]. The assay showed less than 0.15% cross-reactivity with fragments of the heptapeptide and with leucine-enkephalin-containing peptides. Acid acetone extraction of rat striatum followed by Sephadex G-50 chromatography and reverse-phase high pressure liquid chromatography showed that essentially all immunoreactivity co-chromatographed with Met-enkephalin[Arg6,Phe7]. This confirmed the specificity of the assay and showed that the striatum does not contain a high concentration of larger molecular weight forms with the heptapeptide at the COOH terminus. Distribution of the heptapeptide followed that of methionine enkephalin, with highest concentrations in the globus pallidus, intermediate levels in caudate-putamen and hypothalamus, and low levels in cortex and cerebellum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08629.x
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  • 7
    Electronic Resource
    Electronic Resource
    Thermal Denaturation of Native Striatal Tyrosine Hydroxylase: Increased Thermolability of the Phosphorylated Form of the Enzyme (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: Tyrosine hydroxylase was purified from bovine corpus striatum. The native enzyme had a half-life of 15 ± 3 min at 50°C. Phosphorylation of tyrosine hydroxylase with protein kinase purified from both corpus striatum and heart activated the enzyme, but activity was rapidly lost with additional preincubation of the enzyme at 30°C. Thermal denaturation studies indicated that phosphorylated tyrosine hydroxylase had a half-life of 5 ± 2 min at 50°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01641.x
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  • 8
    Electronic Resource
    Electronic Resource
    Met-Enkephalin [Arg6,Phe7] Immunoreactivity in Bovine Caudate and Bovine Adrenal Medulla (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A radioimmunoassay specific for the COOH-terminus of Met-enkephalin [Arg6,Phe7] and a separate assay specific for the COOH-terminus of Met-enkephalin are described. Immunoreactivity by these two assays was compared in bovine caudate and bovine chromaffin granule preparation after Sephadex G75 chromatography in 50% acetic acid. When the assays were applied to the chromatography fractions of the bovine caudate extract, the majority of the immunoreactivity was found in the fractions corresponding to the heptapeptide and the pentapeptide respectively. When the chromaffin granule chromatography fractions were assayed, both of the radioimmunoassays showed that most reactivity was in several peaks in the larger molecular weight fractions. The major peak for the Met-enkephalin [Arg6,Phe7] assay had an apparent molecular weight of 2800, while with the Met-enkephalin assay the dominant peak of immunoreactivity had an apparent molecular weight of 10,000. The presence of authentic Met-enkephalin [Arg6,Phe7] in both caudate and chromaffin granule extracts was confirmed by reverse-phase chromatography of the previously sized fractions. It appears then that the processing of precursors of opioid peptides is directed, in the caudate, to the synthesis and storage of the enkephalins and of Met-enkephalin [Arg6,Phe7]; in the adrenal medulla the major products of precursor processing are a variety of polypeptides of larger sizes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb04713.x
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  • 9
    Electronic Resource
    Electronic Resource
    α-N-Acetyl β-Endorphins in the Pituitary: Immunohistochemical Localization Using Antibodies Raised Against Dynorphin(1-13) (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: Intense immunohistochemical staining of the intermediate lobe of the pituitary was observed by using an antiserum raised against synthetic dynorphin(1-13) treated with a water-soluble carbodiimide (CDI). Subsequent studies showed that the immunostaining was blocked by preincubation of the antiserum with acetylated derivatives of both β-endorphin and dynorphin(1-13) as well as by CDI-treated dynorphin(1-13), but only weakly by authentic dynorphin(1-13). Neither nonacetylated β-endorphin nor any other fragments of the ACTH/endorphin precursor blocked the immunostaining of the intermediate lobe. Analysis of the CDI-treated dynorphin(1-13) used as an antigen showed that most of the peptide was acetylated at primary amino groups. CDI treatment of dynorphin(1-13) results in the formation of an acetyl derivative because the commercially available peptide is supplied as the acetate salt. The antibodies responsible for the intermediate lobe staining were isolated by affinity chromatography, using a column containing partially purified intermediate lobe extract linked to an affinity resin and a radioimmunoassay (RIA) was developed with CDI-treated dynorphin(1-13) used as a trace and as a standard. Competition studies showed 0.5-1% cross-reactivity with α-N-acetyl β-endorphin(1-31), α-N-acetyl β-endorphin(1-27), and totally acetylated β-endorphin(1-31). Nonacetylated β-endorphins did not cross-react. Posterior-intermediate lobe extracts from rat and beef were fractionated by gel filtration. Rat posterior-intermediate lobe extracts were also fractionated by cation-exchange chromatography. Fractionated extracts were analyzed by RIAs for β-endorphin, CDI-treated dynorphin(1-13), and authentic dynorphin(1-13). The results suggested that the peptides responsible for the intermediate lobe staining were mainly four different derivatives of β-endorphin bearing an acetyl group at the amino terminus. No immunostaining was seen in the posterior and anterior lobes of the pituitary. This suggests that the intermediate lobe is the main source of acetylated β-endorphins in the pituitary.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb10823.x
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  • 10
    Electronic Resource
    Electronic Resource
    Tyrosine Hydroxylase from Bovine Striatum: Catalytic Properties of the Phosphorylated and Nonphosphorylated Forms of the Purified Enzyme (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The properties of purified tyrosine hydroxylase (TH) from bovine corpus striatum, both native and phosphorylated forms of the enzyme, were studied. TH had a tendency toward greater affinity for tetrahydrobiopterin (BH4) than for the synthetic cofactor 6-methyltetrahydropterin (6-MPH4), although the maximal velocity of the TH-catalyzed reaction was greater with 6-MPH4. Phosphorylation increased the affinity of TH for cofactor at pH 6.0, with little change in Vmax. At pH 7.0, phosphorylation caused increased activation of TH by increasing Vmax as well as reducing the Km for cofactor. The Km for dopamine was increased twofold by phosphorylation at pH 6.0, but eightfold at pH 7.0. Phosphorylation was not associated with a change in Km for tyrosine at any pH or with any cofactor studied, although the Km for tyrosine of TH was cofactor-dependent and seven to eight times greater with 6-MPH4 than with BH4 as cofactor. Heparin and NaCl activated native TH at pH 6.0, but not at pH 7.0. Phosphorylated TH was unaffected by heparin or salt at pH 6.0, but was relatively inhibited at pH 7.0. The data are presented in the context of the physiological environment of TH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb03962.x
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