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  • 1
    Digitale Medien
    Digitale Medien
    OCCURRENCE OF A SEROTONIN SULPHOTRANSFERASE IN THE BRAIN (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract— —An enzyme catalysing the transfer of sulphate from 3′-phosphoadenylsulphate to serotonin was purified from rabbit brain. The purification procedure involved ammonium sulphate fractionation of the 200,000 g supernatant of rabbit brain homogenate, treatment with alumina Cγ, and chromatography on DEAE-cellulose. The enzyme was purified 67-fold from the 200,000 g supernatant of the brain homogenate. The intracranial distribution of the sulphotransferase was investigated and the cerebellum found to have rather high activity. The sulphotransferase activities of rabbit, dog, rat and bovine brains were compared; rabbit brain had the highest activity, followed by dog, rat and bovine brain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1969.tb06457.x
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  • 2
    Digitale Medien
    Digitale Medien
    Alterations in Catecholamine System Enzymes (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 771 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Allgemeine Naturwissenschaft
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb44677.x
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  • 3
    Digitale Medien
    Digitale Medien
    Interleukin-2 but not basic fibroblast growth factor is elevated in parkinsonian brain (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 1077-1081 
    Details
    ISSN: 1435-1463
    Schlagwort(e): Interleukin-2 ; basic fibroblast growth factor ; Parkinson's disease ; brain
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The contents of interleukin (IL)-2 and basic fibroblast growth factor (bFGF) were measured in the brain (caudate nucleus, putamen, and cerebral cortex) from control and parkinsonian patients by highly sensitive enzyme-linked immunosorbent assay (ELISA). The concentrations of IL-2 in the brain were in the order of pg/mg protein, and the values were significantly higher in the caudate and putamen from parkinsonian patients than those from control patients. However, the levels of IL-2 in the cerebral cortex showed no significant difference between parkinsonian and control patients. In contrast to IL-2, the bFGF levels in the brain were high and in the order of ng/mg protein, and there was no significant difference in the caudate and putamen between parkinsonian and control patients. Although both IL-2 and bFGF may play important roles in dopaminergic neurons as neurotrophic factors, IL-2 but not bFGF may relate to the compensatory response in the nigrostriatal dopaminergic regions in parkinsonian brain during progress of neurodegeneration.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01291792
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  • 4
    Digitale Medien
    Digitale Medien
    Immunocytochemical study of catecholaminergic neurons in the senescence-accelerated mouse (SAM-P8) brain (1997)
    Springer
    Journal of neural transmission 104 (1997), S. 1267-1275 
    Details
    ISSN: 1435-1463
    Schlagwort(e): Catecholamine ; senescence-accelerated mouse (SAM-P8) ; immunocytochemistry ; aging
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The catecholaminergic neurons of senescence-accelerated mice (SAM-P8) were analyzed by immunohistochemical microphotometry in terms of immunoreactivities to aromatic L-amino acid decarboxylase (AADC), dopamine (DA), or noradrenaline (NA). Accelerated senescence-resistant mice (SAM-R1) were used as control mice. The immunoreactivities to AADC, DA, and NA of the catecholaminergic neurons of the SAM-P8 mice were weaker than those of the SAM-R1 mice in all the brain regions. Immunoelectron microscopy revealed progressive degeneration of dopaminergic neurons and their terminal fibers in the substantia nigra as well as in noradrenergic neurons and their proximal dendrites in the locus coeruleus of the SAM-P8 mice. In contrast, there was no difference between the SAM-P8 and SAM-R1 mice in the distribution of AADC-only positive neurons (designated as D neurons in the rat brain by Jaeger et al.) nor in their immunoreactivities. These results may indicate that DA neurons in the substantia nigra and NA neurons in the locus coeruleus degenarate more rapidly during aging in SAM-P8 mice than in control SAM-R1 mice and that D neurons may function as a part of a compensatory system for the decreases in catecholaminergic neurons during aging.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01294727
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  • 5
    Digitale Medien
    Digitale Medien
    Identification of flavin in the purified beef brain mitochondrial monoamine oxidase (1969)
    Springer
    Cellular and molecular life sciences 25 (1969), S. 583-584 
    Details
    ISSN: 1420-9071
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Zusammenfassung Die Monoaminoxydase in den Mitochondrien des Rinderhirns wurde gereinigt. FAD wurde durch Fluoreszenzspektrum und Dünnschichtchromatographie als prosthetische Gruppe in den gereinigten Präparaten identifiziert.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01896523
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  • 6
    Digitale Medien
    Digitale Medien
    Fluorescence assay of tyrosine hydroxylase activity in tissue homogenate (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 1183-1184 
    Details
    ISSN: 1420-9071
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Zusammenfassung Es wird eine Fluoreszenzmethode zur Bestimmung der Tyrosin-Hydroxylase-Aktivität von Homogenat beschrieben, die auf der Spektrofluorometrie der DOPA-Bildung beruht. Die Tyrosin-Hydroxylase-Aktivität von Homogenat der Nebenniere und des Gehirns (Nucleus caudatus) wurde mit dieser Methode gemessen.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02147842
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  • 7
    Digitale Medien
    Digitale Medien
    The effect of high phenylalanine concentration on the formation of DOPA from phenylalanine and tyrosine by tyrosine hydroxylase (1967)
    Springer
    Cellular and molecular life sciences 23 (1967), S. 532-533 
    Details
    ISSN: 1420-9071
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Zusammenfassung Auf der Basis gegenseitiger Hemmung von Phenylalanin konnte die enzymatische Bildung des DOPA über Phenylalanin und Tyrosin mittels Tyrosinhydroxylase untersucht werden. Eine 70%ige Hemmung der enzymatischen DOPA-Bildung ergab sich im Fall der dreissigfachen Konzentration des Phenylalanin. Die Möglichkeit einer Hemmung der Norepinephrin-Bildung in Phenylketonurie wird diskutiert.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02137951
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  • 8
    Digitale Medien
    Digitale Medien
    Hydrolysis of amino acidβ-naphthylamides by aminopeptidases in human parotid saliva and human serum (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 347-348 
    Details
    ISSN: 1420-9071
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Zusammenfassung Die Aktivität der Aminopeptidasen im menschlichen Speichel von Ohrspeicheldrüsen wurde durch Fluoreszenzanalyse gemessen. Die Substratspezifität der Speichelaminopeptidasen war derjenigen der Serumenzyme ähnlich. Das Glycyl-Prolin β-naphthylamidspaltende Enzym war jedoch im Speichel von Ohrspeicheldrüsen in relativ grösserer Menge vorhanden.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02140813
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  • 9
    Digitale Medien
    Digitale Medien
    Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain (1999)
    Springer
    Journal of neural transmission 106 (1999), S. 607-617 
    Details
    ISSN: 1435-1463
    Schlagwort(e): Keywords: Aromatic L-amino acid decarboxylase ; brain ; colocalization ; GTP cyclohydrolase I ; human ; immunohistochemistry ; tetrahydrobiopterin ; tyrosine hydroxylase.
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary. Guanosine triphosphate (GTP) cyclohydrolase I (GCH) is the first and rate-limiting enzyme for biosynthesis of tetrahydrobiopterin, the cofactor of tyrosine hydroxylase (TH). Our previous study reported the presence of GCH in several neuronal groups in animal brains using a newly raised anti-GCH antibody. The present study aims at elucidating whether GCH and TH coexist in the same neurons of the human brain with the aid of immunohistochemical dual labeling. GCH-immunoreactivity was observed in the cell bodies and fibers of monoaminergic neurons of the human brain. Neurons which contain both enzymes are seen in the human substantia nigra, ventral tegmental area, locus coeruleus, dorsal raphe, and zona incerta. In these regions, almost all the cells also show immunoreactivity for aromatic L-amino acid decarboxylase (AADC), the second step enzyme for catecholamine synthesis, indicating that these neurons are catecholaminergic. However, some neurons in the dorsal and dorsomedial hypothalamic nuclei are stained only for GCH or TH. They appear to constitute an independent cell group in the human brain. The present observation suggests that L-dopa is not produced in the cells immunoreactive for TH but not for GCH, and that TH in these cells which lack GCH may have an unidentified role other than dopa synthesis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s007020050183
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  • 10
    Digitale Medien
    Digitale Medien
    Expression of human tyrosine hydroxylase type I in Escherichia coli as a protease-cleavable fusion protein (1999)
    Springer
    Journal of neural transmission 106 (1999), S. 819-824 
    Details
    ISSN: 1435-1463
    Schlagwort(e): Keywords: Human tyrosine hydroxylase type 1 ; N-terminal amino acid-deleted mutant ; maltose-binding protein fusion.
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary. Wild-type and N-terminal 35-, 38-, and 44-amino acid-deleted mutants of human tyrosine hydroxylase type 1 (hTH1) fused to maltose-binding protein via the target sequence for a restriction protease were expressed in Escherichia coli and purified. The fused protein was treated with the restriction protease factor Xa or enterokinase to isolate hTH1 from the fused form. The treatment of fused wild-type and 35-amino acid-deleted mutant with factor Xa and enterokinase caused non-specific cleavages in the vicinity of the phosphorylation sites, Ser19 and Ser40, due to the flexible conformation of the N-terminus of hTH1.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s007020050202
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