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  • 1
    Electronic Resource
    Electronic Resource
    Phosphorus-31 nuclear magnetic resonance studies on serum low and high density lipoproteins. Effect of paramagnetic ion (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 1915-1920 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00680a017
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Benzodiazepine Binding to Cultured Human Pituitary Cells (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 43 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Benzodiazepine receptors were investigated in a cell line of human pituitary cells (18-54,SF) grown in serum-free medium. Preparations of 18–54,SF whole cells and cell membranes were shown to possess satu-rable [3H]diazepam binding sites. Membrane sites were found to have a KD of 20 nM for diazepam while whole cells possessed a twofold higher value. The KD values determined from Rosenthal, Hill, and kinetic analyses were consistent for each preparation. Whole-cell binding of [3H]diazepam was observed to be more stable than binding to membranes at higher temperatures (37°C) and when longer incubation times (60 min) were employed at 4°C. The rank order potency of various benzodiazepines to inhibit [3H]diazepam binding to whole cells and membranes was Ro 5–4864, flunitrazepam, diazepam, and clonazepam. Representatives of other drug classes did not inhibit this benzodiazepine binding. When 18–54,SF cells were grown for 24 h with 100 nM diazepam and then extensively washed membranes prepared, the KD for diazepam increased to 38 nM whereas the Bmax was unchanged when compared with untreated controls. Overall, these findings indicate that pituitary cells possess a peripheral-type benzodiazepine receptor and that the whole cell receptor differs quantitatively when compared with the membrane receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12850.x
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  • 3
    Electronic Resource
    Electronic Resource
    Co-localization of corticotropin releasing factor and vasopressin mRNA in neurones after adrenalectomy (1985)
    [s.l.] : Nature Publishing Group
    Nature 315 (1985), S. 59-61 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] CRF and vasopressin act synergistically to release adrenocor-ticotropic hormone (ACTH) from the anterior pituitary4. Recently, immunohistochemical studies have demonstrated that CRF-containing fibres in the median eminence arise from cells in the parvocellular subdivision of the PVN5, whereas the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/315059a0
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The metabolism and structure of phosphoglycoproteins in rat brain (1982)
    Springer
    Neurochemical research 7 (1982), S. 1243-1256 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Glycoproteins that contain phosphohexosyl groups were found to be present in the myelin- and synaptosomal-enriched fractions as well as in the microsomes of rat brain. The kinetics of flow of intraperitoneally injected [32P]phosphate suggests that the phosphate is enzymatically added in structures found in the microsomal fraction. The newly synthesized phosphoglycoproteins then appear in the soluble fraction of the synaptosomes and in the cytosol, prior to incorporation into the membranes of the synaptosomes and myelin. Phosphoglycopeptides recovered from the phosphoglycoprotein contain 3 Mannose units per N-acetylglucosamine residue; one of the mannose residues is phosphorylated. [13C]NMR studies indicate that the phosphoglycopeptides contain a chitobiose group and more than four sugar residues. Thus, the phosphomannoglycopeptides from rat brain contain an average of 2 N-acetylglucosamine, 6 mannose, and two phosphate moieties per oligosaccharide chain. Enzymatic treatment with α-mannosidase failed to remove the phosphomannose, although some mannose residues were released. Thus, the phosphorylated mannose is not removed by the glycosidase and terminal nonphosphorylated mannose residues are present in the oligosaccharide. The phosphate residues are removed by treatment with alkaline phosphatase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965895
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  • 5
    Electronic Resource
    Electronic Resource
    Distribution of endogenously phosphorylated proteins in subcellular fractions of rat cerebral cortex (1977)
    Springer
    Neurochemical research 2 (1977), S. 533-548 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The cerebral cortex from adult rats was separated into several subcellular fractions by using established methods of differential and sucrose density gradient centrifugation. Aliquots from each fraction were incubated with γ-32P-ATP, in the presence and absence of adenosine 3′,5′-monophosphate (cyclic AMP), and its protein constituents were separated by means of SDS-slab gel electrophoresis. Fractions containing nuclei, synaptosomes, myelin, microsomes, and soluble proteins each showed a characteristic pattern of protein staining and of endogenously phosphorylated proteins detected by autoradiography of the gels. Cyclic AMP-stimulated phosphorylation of proteins with MW 78K and 84K can serve as markers for membranes of synaptic origin, while cyclic AMP-independent phosphorylation of low-molecular-weight proteins (15K–20K) is characteristic of myelin. The finding of different phosphoproteins in various subcellular fractions may be related to the diversity of cellular functions known to be regulated by phosphorylative activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00966013
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    In situ hybridization of putative somatostatin mRNA within hypothalamus of the rat using synthetic oligonucleotide probes (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 415-422 
    Details
    ISSN: 0730-2312
    Keywords: in situ hybridization ; somatostatin ; mRNA ; immunocytochemistry ; hypothalamus ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The distribution of mRNA with high sequence homology to somatostatin mRNA within the periventricular hypothalamus of rat was assessed using in situ hybridization techniques with synthetic oligodeoxyribonucleotide probes, complementary to the 3′ coding region of rat somatostatin mRNA. The probes (22- and 24-mers) were 5′-end labeled using T4 polynucleotide kinase and γ-32P-ATP. They were used either individually or after ligation with T4 DNA ligase to form a 46-mer. Serial tissue sections ( 〈 10 μm) were taken from the level of the preoptic/anterior hypothalamus through the paraventricular hypothalamus. In situ hybridizations were conducted at room temperature in hybridization buffer. Neurons immuno-reactive with antiserum raised against somatostatin were identified in alternate sections using standard immunocytochemical procedures. The anatomical location of the hybridization signal was determined by autoradiography. Our results show that the peri- and paraventricular hypothalamus is rich in transcripts putatively coding for somatostatin and that these transcripts are co-distributed with neurons immunoreactive with antisomatostatin immunoglobulin.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270410
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