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  • 1
    Electronic Resource
    Electronic Resource
    Quaternary Structure of the Native GABAA Receptor Determined by Electron Microscopic Image Analysis (1994)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 62 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: In the transmitter-gated ion channel class of receptors, the members of which are all believed to be heterooligomers, the number and arrangement of the subunits are only known with any certainty for the nicotinic acetylcholine receptor from Torpedo electric fish. That receptor has been shown to possess a pentameric rosette structure, with five homologous subunits (α2βγδ) arranged to enclose the central ion channel. The data were obtained by electron image analysis of two-dimensional receptor arrays, which form as a consequence of that receptor's exceptionally high abundance in the Torpedo membranes and are therefore not attainable for other receptors. We have applied another direct approach to determine the quaternary structure of native ionotropic GABA receptors. We have purified those receptors from porcine brain cortex and analysed the rotational symmetry of isolated receptors visualized by electron microscopy. The results show the receptor to have a pentameric structure with a central water-filled pore, which can now be said to be characteristic of the entire superfamily.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.62020815.x
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  • 2
    Electronic Resource
    Electronic Resource
    Agonist-Selective Protection of the Opioid Receptor-Coupled G Proteins from Inactivation by 5′-p-fluorosulphonylbenzoyl Guanosine (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 54 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The guanine nucleotide analogue, 5′-p-fluorosul-phonylbenzoyl guanosine (FSBG), can react covalently with GTP-binding proteins (G proteins). In rat brain membranes, FSBG causes a time-dependent loss of β,γ-imido[8-3H]guanosine 5′-triphosphate binding sites. Using 1 mM FSBG, the guanyl nucleotide modulation of opioid agonist binding is abolished, whereas the guanyl nucleotide sensitivity of neurotensin binding is retained. The action of FSBG can be prevented by the presence of opioid agonists, but not the antagonist naloxone. Iodoacetamide treatment of membranes in the presence of agonist, but not antagonist, can attenuate the action of FSBG in blocking guanyl nucleotide modulation of opioid agonist binding. These results suggest that FSBG covalently modifies essential thiol groups, whose exposure to the reagent is modified by agonist occupancy of the receptor, on a species of G protein linked to opioid receptors, but not on a species of G protein linked to neurotensin receptors. Thus, FSBG may have selectivity for the forms of Gi or Go, proteins associated with opioid receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb13280.x
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of Neurotensin Binding Sites in Intact and Solubilized Bovine Brain Membranes (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Analysis of the equilibrium binding of [3H]-neurotensin(1–13) at 25°C to its receptor sites in bovine cortex membranes indicated a single population of sites with an apparent equilibrium dissociation constant (KD) of 3.3 nM and a density (Bmax) of 350 fmol/mg protein (Hill coefficient nH= 0.97). Kinetic dissociation studies revealed the presence of a second class of sites comprising 〈10% of the total. KD values of 0.3 and 2.0 nM were obtained for the higher and lower affinity classes of sites, respectively, from association-dissociation kinetic studies. The binding of [3H]neurotensin was decreased by cations (monovalent and divalent) and by a nonhydrolysable guanine nucleotide analogue. Competition studies gave a potency ranking of [Gln4]neurotensin 〉 neurotensin(8–13) 〉 neurotensin(1–13). Smaller neurotensin analogues and neurotensin-like peptides were unable to compete with [3H]neurotensin. Stable binding activity for [3H]neurotensin in detergent solution (KD= 5.5 nM, Bmax= 250 fmol/mg protein, nH= 1.0) was obtained in 2% digitonin/l mM Mg2+ extracts of membranes which had been preincubated (25°C, 1 h) with 1 mM Mg2+ prior to solubilization. Association-dissociation kinetic studies then revealed the presence of two classes of sites (KD1= 0.5 nM, KD2= 3.6 nM) in a similar proportion to that found in the membranes. The solubilized [3H]-neurotensin activity retained its sensitivity to cations and guanine nucleotide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb02998.x
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  • 4
    Electronic Resource
    Electronic Resource
    Size of acetylcholine receptors in the membrane. An improved version of the radiation inactivation method (1982)
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 2210-2217 
    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/bi00538a033
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  • 5
    Electronic Resource
    Electronic Resource
    Ribonucleases (1969)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 38 (1969), S. 677-732 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.38.070169.003333
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  • 6
    Electronic Resource
    Electronic Resource
    A Cytochemical Reaction for Nucleoprotein (1956)
    [s.l.] : Nature Publishing Group
    Nature 178 (1956), S. 1450-1453 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] WE have recently completed a study of a cytochemical reaction for protein which appears to be specific for protein in a special form of combination with nucleic acid. When a diazonium hydroxide is applied to a tissue section, the following components may react: (1) tyrosine and histidine and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1781450a0
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Parallel regulation of acetylcholinesterase and pseudocholinesterase in normal, denervated and dystrophic chicken skeletal muscle (1979)
    [s.l.] : Nature Publishing Group
    Nature 280 (1979), S. 160-162 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It has been reported12'15 that embryonic chick muscle has high AChE concentrations which fall during maturation, but those studies used conditions of no or low salt or detergent, which are now known8'11'16'17 to give low AChE extraction. We have homogenised the tissues in 1% Triton X-100/1M NaCl, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/280160a0
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  • 8
    Electronic Resource
    Electronic Resource
    The density of cholinergic receptors at the endplate postsynaptic membrane: Ultrastructural studies in two mammalian species (1975)
    Springer
    The journal of membrane biology 20 (1975), S. 31-49 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Electron-microscope autoradiography of diaphragm endplates of the American brown bat, labeled to saturation with tritiated α-bungarotoxin, has been used as a means to localize and quantitate the acetylcholine receptor there. Analysis of the grain distribution in these autoradiographs reveals that the receptor sites in this endplate are located on the postsynaptic membrane at an average density of 8,800/μ2. The sites are distributed asymmetrically along that membrane, being concentrated at the crests of the postjunctional folds—that portion nearest to the presynaptic membrane. The receptor site density at these regions of the postsynaptic membrane is estimated to be 20,000–25,000/μ2 of membrane surface. A comparison of these membrane site densities with those of endplates of red and white fibers of the mouse reveals a close similarity. On this basis, it is suggested that the receptor site density at the crests of the folds may be a characteristic feature of endplates of vertebrates. In contrast to the acetylcholine receptor sites, cholinesterase sites (determined autoradiographically in3H-diisopropylfluorophosphate-labeled endplates) are largely distributed in a uniform manner over the postjunctional folds. The function of the secondary folds is, therefore, reassessed. Ultrastructural evidence available from other laboratories on the spatial characteristics of transmitter release and of postsynaptic dense particles is in accord with a model drawn for this molecular architecture at the vertebrate endplate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870626
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  • 9
    Electronic Resource
    Electronic Resource
    The ultrastructural localization and quantitation of cholinergic receptors at the mouse motor endplate (1973)
    Springer
    The journal of membrane biology 14 (1973), S. 383-402 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The snake venom toxin, α-bungarotoxin, is known to bind specifically to the acetylcholine receptor at skeletal muscle endplates. In this study, tritiated α-bungarotoxin has been used in conjunction with electron-microscope autoradiography to visualize and enumerate acetylcholine receptor sites at the neuromuscular junctions of the mouse diaphragm. From an analysis of the grain distribution, the receptor sites appear to be located specifically on the postjunctional membrane. The density there is about 8,500/μ2 of membrane surface. For comparison purposes, cholinesterases and related active centers were labeled using [3H] diisopropylfluorophosphate; they were shown to be at this same concentration over the synaptic membranes (or along the cleft). The 1∶1 relationship of the receptors to the cholinesterase type of site, found previously to hold in studies on whole endplates, is also true at the ultrastructural level in this case. In fact, this 1∶1 relationship is believed to be a characteristic of the postsynaptic membranes of endplates in other muscles and other vertebrates. Based on the constant density value thus arrived at, the total surface areas of postsynaptic and of presynaptic membranes are at once obtained from the known total numbers of these sites per endplate, available from previous studies in this laboratory. Examples of such synaptic surface area values are given. These values are only reliable for a given muscle type if the approximate fiber size is defined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868086
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of functional GABA, glycine and glutamate receptors in Xenopus oocytes injected with rat brain mRNA (1984)
    [s.l.] : Nature Publishing Group
    Nature 310 (1984), S. 318-321 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] mRNA was extracted from day 14 Wistar (WA/KIR) rats using a guanidinium thiocyanate method6. Poly(A) mRNA was isolated by oligo(dT)-cellulose chromatography and injected into Xenopus laevis oocytes (40ng per cell) as previously reported4. After microinjection of the mRNA, cells were maintained in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/310318a0
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