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  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic Reconstitution of Brain Membrane and Membrane Opiate Receptors (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 46 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A new method using lysophosphatide and acyl-CoA as detergents has been used to solubilize the rat brain opiate receptor. After solubilization, lysophosphatide and acyl-CoA can be almost completely removed by an enzymatic reaction that uses an acyltransferase from rat liver microsomes and reconstitutes the solubilized receptor in membranous vesicles. Morphological studies performed with negative staining and freeze-fracture electron microscopy revealed that the general appearance and intramembrane particle distribution of fracture faces in the reconstituted membrane are similar to those of the native membrane; this indicates that hydrophobic protein components of the original membrane were incorporated during reconstitution. Reconstituted membrane, however, contained higher levels of phosphatidylcholine and lower levels of cholesterol. The activities of the membrane-bound enzymes Na+, K − -ATPase and Ca2 -, Mg2+-ATPaxe in the reconstituted system were 24 and 3%, respectively, those of the native membrane. Although binding of opiate ligands to the reconstituted membrane was stereospecific and saturable, higher concentrations of some of the unlabeled ligands were required to inhibit binding of the radiolabeled ligands. These changes in receptor characteristics are likely due to changes in lipid composition, physical state, and/or distribution of the lipids in the reconstituted membrane bilayer. This conclusion is supported by an increase in the affinity of opiate ligands for reconstituted membrane after adjustment of the latter's lipid composition to match more closely that of the original membrane. This was accomplished by treatment with phospholipid exchange protein to remove the excess phosphatidylcholine and by incorporation of cholesterol into the reconstituted membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb13062.x
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  • 2
    Electronic Resource
    Electronic Resource
    Lipid Requirement for μ Opioid Receptor Binding (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 49 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We have previously shown that a partially purified μ opioid receptor from bovine brain requires lipids to exhibit full binding activity. In the present report, we have determined the specificity of this lipid requirement. Lipids active in this regard were found always to contain an acidic head group and a fatty acid with two or more double bonds. Free, polyunsaturated fatty acids were also able to confer high binding activity on the partially purified opioid receptor. The possible roles lipids play in opioid binding are discussed in light of these data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb09987.x
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  • 3
    Electronic Resource
    Electronic Resource
    Mouse Brain DNA-Dependent RNA Polymerases After Chronic Morphine Treatment (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Chronic morphine pellet implantation was found to decrease the specific activity of two forms of mouse brain RNA polymerase I and to alter the requirements of Mg2+ and Mn2+ for the activities of RNA polymerases II and III. DNA-dependent RNA polymerases were partially purified from small dense nuclei isolated from brains of naive and morphine tolerant-dependent mice, and three RNA polymerases were separated on a DEAE-Sephadex A-25 column. The three fractions, referred to as peak I, peak II, and peak III, were studied, characterized, and identified as being RNA polymerases I, II, and III, respectively. Chronic-morphine pellet implantation resulted in a lower specific activity of RNA polymerase I, but the specific activities of RNA polymerases II and III were not affected. This effect was prevented by preimplantation of a naloxone pellet and thus was narcotic-specific. Chronic morphine treatment lowered the concentration of Mg2+ required for optimal activity of RNA polymerase II and elevated the Mn2+-Mg2+ activity ratios of RNA polymerases II and III. A second DEAE-Sephadex A-25 column chromatography of the peak I RNA polymerase was carried out, revealing five component activity peaks. Two of these contained lower specific activities as a result of chronic morphine pelletimplantation. These specific changes in RNA polymerase function in morphine tolerance-dependence may be associated with the elevated chromatin template activities, altered chromatin phosphorylation, and elevated rates of cell-free translation that have been reported by others.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb09939.x
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  • 4
    Electronic Resource
    Electronic Resource
    Partial Purification of Nuclear Protein Kinase from Small Dense Nuclei of Mouse Brain and the Effect of Chronic Morphine Treatment (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: To deduce whether or not the nuclear protein kinase activity may be responsible for the change in phosphorylation of chromatin proteins during morphine tolerance-dependence, the nuclear protein kinases from small dense nuclei of mouse brain have been partially purified by ammonium sulfate fractionation and phosphocellulose column chromatography. Two peaks of cyclic AMP-independent nuclear protein kinase activity are eluted from the phosphocellulose column by a linear NaCl gradient. During morphine tolerance-dependence, the specific activity of peak I, but not of peak 11, is increased significantly relative to placebo controls. This increase in nuclear protein kinase activity may partially account for the elevated chromatin protein phosphorylation in small dense nuclei of mouse brain seen during morphine tolerance-dependence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb09971.x
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  • 5
    Electronic Resource
    Electronic Resource
    Enzymic synthesis of D-alanyl-D-alanine. IV. Control of D-alanine: D-alanine ligase (ADP) (1969)
    s.l. : American Chemical Society
    Biochemistry 8 (1969), S. 5119-5124 
    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/bi00840a066
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  • 6
    Electronic Resource
    Electronic Resource
    Mathematical modeling of opiate binding to mouse brain membrane (1985)
    Springer
    Bulletin of mathematical biology 47 (1985), S. 503-512 
    Details
    ISSN: 1522-9602
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Mathematics
    Notes: Abstract The heterogeneity of rat brain opiate receptors was examined by analyzing competition data. The binding of three prototypical tritiated opioid agonists, [3H]-dihydromorphine ([3H]-DHM), [3H]-D-ala2-D-leu5-enkephalin ([3H]-DADLE), and [3H]-ethylketocyclazocine ([3H]-EKC) was determined in the presence of varying concentrations of each of these unlabeled ligands, generating nine displacement curves. A computer program was then used to find the best fit of a model system to these data, assuming two, three or four independent binding sites. The best fit was a four-site model. One of these sites is specific for DHM; two are relatively selective for DHM and DADLE respectively, but also bind EKC. The remaining site binds only EKC with high affinity. These results, together with displacement data using naloxone, FK33824, and D-ala2-met5-enkephalinamide, are discussed in terms of current opiate receptor models.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02460010
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  • 7
    Electronic Resource
    Electronic Resource
    Dynorphin(1–13) improves survival in cats with focal cerebral ischaemia (1984)
    [s.l.] : Nature Publishing Group
    Nature 312 (1984), S. 551-552 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Forty-two adult male cats (3-5 kg) assigned randomly to one of four groups were anaesthetized with halothane and subjected transorbital occlusion of the right middle cerebral artery16. A subcutaneouspocket was created for later placement of an osmotic pump through a small midline lumbar incision, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/312551a0
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  • 8
    Electronic Resource
    Electronic Resource
    Opioid-binding protein (OBCAM) is rich in β-sheets (1990)
    Springer
    The protein journal 9 (1990), S. 3-7 
    Details
    ISSN: 1573-4943
    Keywords: Opioid-binding proteins ; conformation ; circular dichroism ; sequence-predictive method
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23–30 and 83–93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024977
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  • 9
    Electronic Resource
    Electronic Resource
    Genetic mapping of opioid binding protein gene(s) to mouse Chromosome 9 (1993)
    Springer
    Mammalian genome 4 (1993), S. 179-182 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352235
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