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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: 3α-Hydroxysteroid oxidoreductase (EC 1.1.1.50) was localized in the rat brain by cryostat sectioning, microassay, and neurochemical lesions. Single 16-μm sections were cut, homogenized, and assayed. In the olfactory tubercle 3α-hydroxysteroid oxidoreductase activity is high in the piaglial layer at the surface, 20-fold lower at a depth of 50 μm, and 50-fold lower at a depth of 200 μm. A similar pattern of activity was seen in the olfactory bulb, the interpeduncular nucleus, the frontal pole of the cortex, and the frontoparietal cortex. When kainic acid, a toxin that destroys neurons but leaves glia and axons of passage intact, was injected into the olfactory tubercle, 3α-hydroxysteroid oxidoreductase activity was undiminished whereas glutamic acid decarboxylase activity was reduced by 80%. This laminar distribution and insensitivity to kainic acid are consistent with a nonneuronal localization. The high concentration of astrocytes in the pia–glial layer, where 3α-hydroxysteroid oxidoreductase activity is highest, leads us to suggest that this enzyme is localized to astrocytes. The presence of particular enzymes in some brain regions and not in others determines which products are synthesized and which are inactivated in those regions. Thus, the location of 3α-hydroxysteroid oxidoreductase and other steroid converting enzymes can affect the activity of neuronal circuits and the behaviors regulated by those circuits.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 96 (1974), S. 3714-3716 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We describe a simple procedure for the microassay of testosterone 5α-reductase in homogenates of rat brain. This enzyme converts testosterone to dihydrotestosterone. We have used this assay to characterize the enzymatic activity and to map its distribution. The apparent Km is 4.1 × 10−6 M and the Vmax is 85.6 pmol/mg protein/h. The pH optimum is broad and extends from pH 6.0 to 8.0. For the brain regions surveyed, testosterone 5α-reductase activity varied over a 10-fold range. The highest activities were observed in homogenates of the midbrain and pons (37–39 pmol/mg protein/h). The lowest were seen in homogenates of the thalamus, caudate nucleus, frontal cortex, hippocampus, hypothalamus, olfactory tubercle, and preoptic area (3–7 pmol/mg protein/h).
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We describe a simple procedure for the microassay of 3α-hydroxysteroid oxidoreductase in homogenates of rat brain. This enzyme converts dihydrotestosterone to 3α-androstandiol. We have mapped the distribution of the enzymatic activity in 14 regions of the rat brain. The highest activities were observed in homogenates of olfactory bulb (51/nmol/mg protein/h) and olfactory tubercle (29 nmol/mg protein/h). Substantially lower values were seen in the other brain regions, including thalamus, caudate nucleus, frontal cortex, hippocampus, hypothalamus, and preoptic area (6–20 nmol/mg protein/ h).
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 278 (1979), S. 41-43 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1 Summary of CuO-NaOH oxidation of coal* Wt % of productst Lignite Bituminous Organic acid (benzene-ether extract) 35.3 19.6 Humic acid-like material (methanol 54.3 61.0 extract) Non-oxidised coal ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 257 (1975), S. 378-380 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1 Aromatic acids found in the aqueous Na2Cr2O7 oxidation of coal, and identified as methyl esters Number of Precise mass (M-OCH3)+ Relative* abundance Nucleus -COOCH3 Elemental composition Observed Deviation x 103 (±15-20%) Benzene 2 C9H703 163.0400 0.6 38 ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 275 (1978), S. 116-118 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Freshly ground raw lignite from Sheridan, Wyoming was first treated with 5% aqueous HC1 at room temperature to free the acids from the minerals1, and then extracted with 2.5% aqueous sodium hydroxide at 35 °C for 16 h. After work up by the usual method1, soluble organic acids equal to 2.6% by ...
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 44 (1990), S. 229-239 
    ISSN: 0730-2312
    Keywords: adrenocortical carcinoma cells ; protein purification ; anchorage independent growth ; epithelial cell proliferation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A polypeptide growth factor has been partially purified from medium conditioned by the human adrenocortical carcinoma cell line SW13. This factor, designated h-TGFe, stimulates anchorage-independent growth of the SW13 cells. Similar activity was observed in human milk, and in conditioned media from seven of 14 epithelial cell lines. The SW13-derived activity is stable to low pH and 8M urea but labile to dithiothreitol and 2% sodium dodecyl sulfate. Human TGFe does not bind to heparin and fails to stimulate growth of endothelial cells in monolayer culture. The apparent molecular weight of h-TGFe is 59k by size exclusion chromatography in the presence of 8M urea and the activity binds strongly to cation exchangers. The activity elutes at 15-30% acetonitrile from a C18 reversephase column and has been partially purified by using a four-step chromatographic procedure. TGFe appears to be a novel growth factor produced by many epithelial cells and tissues.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 11 (1976), S. 383-387 
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fluorination of bituminous coal by elemental fluorine yields a solid product from which a solid distillate can be made by vacuum pyrolysis. Both fluorinated materials are easily made and are useful for mass spectrometric unit mass assignments. They have certain advantages over the commonly used perfluorokerosene, particularly for use in the high mass region.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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