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  • 1980-1984  (6)
  • 1970-1974  (11)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 54 (1981), S. 253-256 
    ISSN: 1432-0533
    Keywords: Striatonigral degeneration ; Alzheimer's disease ; Parkonsonism ; Dementia ; Tyrosine hydroxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An autopsy case with clinical features of progressive parkinsonism and dementia of presenile occurrence was characterized by the following neuropathologic findings: (1) severe degeneration in the striationigral system and (2) widespread occurrence of numerous senile plaques and Alzheimer's neurofibrillary tangles in the cerebral cortex. We believe this to be a very rare case of striatonigral degeneration combined with Alzheimer's disease, because, as far as we know, only two similar cases have been reported and they had not such typical characteristics of Alzheimer's disease as ours did. In addition, in our case the biochemical examination revealed that the activity of one of the dopamine-synthesizing enzymes, tyrosine hydroxylase, was greatly decreased in the nigro-striato-pallidal system.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 26 (1970), S. 252-253 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Die Aktivität der Aminopeptidasen in Ohrspeicheldrüsen wurde gemessen. Glycyl-Prolinβ-naphthylamid, Alaninβ-naphthylamid, Leucinβ-naphthylamid, Methioninβ-naphthylamid, und Argininβ-naphthylamid wurden von der Mikrosomenfraktion und der löslichen Fraktion schnell gespalten. Das Glycyl-Prolinβ-naphthylamid spaltende Enzym war in Ohrspeicheldrüsen in relativ grösserer Menge vorhanden. Die Aufspaltung von Glycyl-Prolinβ-naphthylamid in Glycyl-Prolin undβ-Naphthylamin wurde papierchromatographisch nachgewiesen.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 26 (1970), S. 722-723 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Die subzelluläre Lokalisation von Tyrosin-Hydroxylase und Monoaminoxydase im Nucleus caudatus des Rindergehirns wurde untersucht. Tyrosin-Hydroxylase fand sich grösstenteils in den Synaptosomen, den Mikrosomen und dem Zytoplasma. Eine bedeutende Aktivität von Monoaminoxydase war in den Mitochondrien vorhanden.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 27 (1971), S. 1399-1399 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung In der löslichen Fraktion der Rinderzahnpulpa wurde die Aminoxydase gereinigt und die Enzymaktivität durch Isoniazid, Cuprizon,p-Chloromercuribenzoat,β-Aminoproprionitril und Lysin-Vasopressin gehemmt. Die Aminoxydase hat wahrscheinlich Kupfer und Pyridoxalphosphat als prosthetische Gruppen.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 37 (1981), S. 809-811 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We describe a highly sensitive assay method for tyrosine hydroxylase (TH) using high-performance liquid chromatography with amperometric determination. This assay method could be applicable to any tissues with low enzyme activity, such as rat cerebellum. We also describe the kinetic properties of TH in rat cerebral cortex.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Neonatal changes in the activities of tyrosine hydroxylase (TH) and tryptophan hydroxylase (TrpH) and in the content of the co-factor, biopterin, were studied in rat midbrain for the first 20 days after birth. Changes in TH activity in the parotid and submandibular glands were also examined. Changes in TH activity per unit weight in the developing rat brain were briefly similar to those in the salivary glands: the activity increased from day 2 or 4 to day 9 after birth, and remained constant or slightly decreased at day 12, then rapidly increased on day 16. TrpH activity in the midbrain increased about twofold up to day 16. The biopterin concentration in the brain increased, reached a maximum level on day 12 after birth, and thereafter decreased. The effect of hyperthyroidism in rats given 0.2 mg/kg i.p. of thyroxine every 2 days postnatally was studied on the activity of TH in rat salivary glands at 12-day-old rats. In parotid or submandibular gland of hyperthyroid rats, TH activity increased at day 12 postnatally. In comparison with the effect on TH activity in the salivary glands, TH activity in the midbrain on day 20 postnatally was not induced by hyperthyroidism. Furthermore, increase of the TrpH activity and biopterin and catecholamine levels in the midbrain of hyperthyroid rats was not found on day 20 after birth in comparison with the corresponding controls. From these data, we suppose that postnatal hyperthyroidism may cause precocious induction of TH in rat salivary gland, but may not increase the activity of TH or TrpH, and the level of their co-factor, biopterin, in rat midbrain.
    Type of Medium: Electronic Resource
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  • 7
    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: Approximately 80 per cent of tyrosine hydroxylase activity in bovine caudate nucleus was particle-bound. The rest of the activity was found in the soluble fraction. The enzyme activity in crude tissue preparations was inhibited, probably by the presence of endogenous inhibitors. Dilution of crude tissue preparations such as the crude mitochondrial fraction caused an increase in the specific activity. The particle-bound enzyme was solubilized by incubation with trypsin. The presence of deoxycholate increased the degree of solubilization. The activity of the solubilized enzyme from the washed particles was also inhibited, but the subsequent purification by ammonium sulphate could eliminate the inhibition. The solubilized enzyme was partially purified by ammonium sulphate fractionation and Sephadex G-150 chromatography. A tetrahydropteridine and ferrous ion were required as cofactors for the partially purified enzyme. Among various divalent cations, only ferrous ion could activate the partially purified enzyme. The enzyme was inhibited by L-α-methyl-p-tyrosine and catecholamines such as dopamine. The optimum pH was found between 5.5 and 6.0. Km values toward tyrosine, 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine and Fe2+, were approximately 5 × 10−5 M, 1 × 10−4 M and 4 × 10−4 M, respectively.
    Type of Medium: Electronic Resource
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  • 8
    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: Abstract— Monoamine oxidase was purified approximately 40-fold from beef brain mitochondria. The purification procedure involved extraction with a non-ionic detergent (Nonion NS-210) after heat treatment, ammonium sulphate fractionation, chromatographies on DEAE-cellulose and Sepharose 6B, and a continuous flow electrophoresis. A major component (enzyme 1) with a higher specific activity and a minor component (enzyme 2) with a lower specific activity were separated. Properties of both enzymes towards kynuramine including pH-optimum and Km values were similar, but the enzyme 1 had the higher specific activity towards tyramine whereas that of enzyme 2 was towards normetane-phrine. Fluorescence spectra indicated that the enzyme 1 is a flavoprotein. Copper was not detected, and copper chelating agents did not inhibit the enzyme. p-Chloromercuribenzoate and JV-ethylmaleimide inhibited the enzyme, indicating the presence of the essential SH-groups.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 28 (1972), S. 905-906 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Es wird gezeigt, dass die Dopamin-β-Hydroxylase-Aktivität im Serum bei spontan hypertonischen Ratten im Vergleich zu normotonen Kontrollen nicht verändert ist.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 28 (1972), S. 634-634 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Nachweis, dass Fusarinsäure die DOPA-Oxydation durch Melanom-Tyrosinase kompetitiv mit DOPA hemmt.
    Type of Medium: Electronic Resource
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