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  • Compositae  (4)
  • CD  (2)
  • Ca current  (2)
  • Cyclic adenosine monophosphate  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Cell cultures of Centaurea cyanus produce malonated anthocyanin in UV light
    Amsterdam : Elsevier
    Phytochemistry 26 (1987), S. 2261-2263 
    Details
    ISSN: 0031-9422
    Keywords: Centaurea cyanus ; Compositae ; UV light ; induction ; malonated anthocyanin. ; suspension culture
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0031-9422(00)84696-8
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  • 2
    Electronic Resource
    Electronic Resource
    Pelargonidin 3-(6''-succinyl glucoside)-5-glucoside from pink Centaurea cyanus flowers
    Amsterdam : Elsevier
    Phytochemistry 27 (1988), S. 1228-1229 
    Details
    ISSN: 0031-9422
    Keywords: Centaurea cyanus ; Compositae ; acylated anthocyanin ; pink flowers ; succinic acid.
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(88)80316-9
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  • 3
    Electronic Resource
    Electronic Resource
    Identification and distribution of malonated anthocyanins in plants of the compositae
    Amsterdam : Elsevier
    Phytochemistry 25 (1986), S. 1337-1342 
    Details
    ISSN: 0031-9422
    Keywords: Cichorium, Dahlia, Helenium ; Compositae ; FAB-MS. ; acylated anthocyanins ; cyanidin 3-malonylglucuronosylglucoside ; dimalonates ; monomalonates
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0031-9422(00)81285-6
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  • 4
    Electronic Resource
    Electronic Resource
    Induction of anthocyanin synthesis and related enzyme activities in cell cultures of Centaurea cyanus by UV-light irradiation
    Amsterdam : Elsevier
    Phytochemistry 30 (1991), S. 2271-2273 
    Details
    ISSN: 0031-9422
    Keywords: Centaurea cyanus ; Compositae ; UV-Iight. ; cell cultures ; chalcone ; chalcone synthase ; flavanone isomerase ; phenylalanine ammonialyase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(91)83628-X
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Secondary structural changes of non-reduced and reduced ribonuclease A in solutions of urea, guanidine hydrochloride and sodium dodecyl sulfate
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 957 (1988), S. 340-344 
    Details
    ISSN: 0167-4838
    Keywords: CD ; Carboxamidomethylated RNAase A ; Guanidine ; RNAase A ; SDS ; Secondary structure
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(88)90223-3
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  • 6
    Electronic Resource
    Electronic Resource
    Effects of prostaglandins E"1 and E"2 on cultured smooth muscle cells and strips of rat aorta
    Amsterdam : Elsevier
    Prostaglandins 47 (1994), S. 353-365 
    Details
    ISSN: 0090-6980
    Keywords: Ca current ; Prostaglandins ; patch clamp ; rat oarta ; smooth muscle cell ; vasodilation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0090-6980(94)90053-1
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  • 7
    Electronic Resource
    Electronic Resource
    Inhibition of nicotinic acetylcholine receptor channels in bovine adrenal chromaffin cells by Y3-type neuropeptide Y receptors via the adenylate cyclase/protein kinase A system (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 351 (1995), S. 337-347 
    Details
    ISSN: 1432-1912
    Keywords: Key words Neuropeptide Y ; Catecholamines ; Cyclic adenosine monophosphate ; Chromaffin cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The effect of neuropeptide Y [NPY(1–36)] and related peptides on the voltage-dependent currents and the nicotinic acetylcholine receptor (nAChR) currents (IACh) of bovine adrenal chromaffin cells was investigated using the whole-cell patch clamp technique. Catecholamine release from single chromaffin cells was measured by means of fast cyclic voltammetry. The potency order of these peptides in inhibiting IACh evoked by nicotine was NPY(1–36), NPY (16–36)〉peptide YY(PYY)〉[Leu31, Pro34]NPY. NPY(16–36) produced a similar degree of inhibition, irrespective of whether nicotine or an equipotent concentration of acetylcholine was used to evoke IACh. NPY(16–36) failed to alter voltage-dependent inward or outward currents. Intracellular cAMP, and extracellular dibutyryl-cAMP, produced a slowly developing increase in IACh. Intracellular cAMP, extracellular 8-Br-cAMP or dibutyryl-cAMP, and an inhibitor of cyclic nucleotide phosphodiesterases 3-isobutyl-1-methyl-xanthine (IBMX), decreased the inhibitory effect of NPY(16–36) on IACh. Although the intracellular application of the cAMP-dependent protein kinase A inhibitor [PKI(14–24)amide] alone did not alter IACh, it potentiated the effect of NPY(16–36) in interaction experiments. While the NPY(16–36)-induced inhibition of IACh was reversed on washout of the peptide, the slightly shorter C-terminal fragment NPY(18–36) caused a long-lasting depression of both IACh and catecholamine secretion evoked by nicotine. This depression was smaller in the presence of extracellular 8-Br-cAMP than in its absence. NPY(18–36) did not alter the secretory activity induced by a high concentration of potassium. It appears that, by activating Y3-receptors, NPY inhibits nAChR-current and the resulting secretion of catecholamines from bovine chromaffin cells. This process may involve a G protein-mediated decrease in intracellular cAMP with a subsequent decrease in the degree of phosphorylation of the nAChR-channel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169073
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Voltage-activated potassium, but not calcium currents in cultured bovine aortic endothelial cells (1987)
    Springer
    Pflügers Archiv 410 (1987), S. 385-393 
    Details
    ISSN: 1432-2013
    Keywords: Bovine aortic endothelial cells ; Patch clamp ; Inward rectifier ; Transient outward K current ; Ca current ; Endothelium-derived relaxing factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The electrophysiological properties of cultured bovine aortic endothelial cells were characterized using the patch clamp technique. Resting potentials were measured on passing to the whole cell recording configuration and were close to −65 mV in healthy cells. In cell-attached recordings with a high potassium pipette solution, inward single channel currents were observed with zero applied pipette potential. A linear slope conductance of 25 pS was found for a wide range of hyperpolarizing patch potentials and also for depolarizing patch potentials of up to 50–60 mV. A pronounced inward rectification was apparent as no reversal of these currents was seen for larger depolarizations. Whole cell recording in physiological solutions revealed the presence of a hyperpolarization-activated inward current with strong inward rectification and no voltage-dependent ionic current was observed upon depolarization in this subset of cells. Substitution of potassium for external sodium resulted in a shift in the zero current potential consistent with potassium being the main permeant ion. Together with the characteristic voltage-dependent blocking actions of external sodium ions and low concentrations of barium and caesium ions, our results indicate that this current is very similar to the classical inward rectifier as originally described in skeletal muscle and in tunicate eggs. In a second population of cells, a depolarization-activated outward current displaying characteristics of the fast transient A-type potassium current as first reported in molluscan neurones was also observed. No evidence for inward voltage dependent sodium or calcium currents was found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00586515
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of nicotinic acetylcholine receptor channels in bovine adrenal chromaffin cells by Y3-type neuropeptide Y receptors via the adenylate cyclase/protein kinase A system (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 351 (1995), S. 337-347 
    Details
    ISSN: 1432-1912
    Keywords: Neuropeptide Y ; Catecholamines ; Cyclic adenosine monophosphate ; Chromaflin cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effect of neuropeptide Y [NPY(1–36)] and related peptides on the voltage-dependent currents and the nicotinic acetylcholine receptor (nAChR) currents (IACh) of bovine adrenal chromafptn cells was investigated using the whole-cell patch clamp technique. Catecholamine release from single chromaffin cells was measured by means of fast cyclic voltammetry. The potency order of these peptides in inhibiting IACh evoked by nicotine was NPY(1–36), NPY (16–36) 〉 peptide YY(PYY) 〉 [Leu31, Pro34] NPY. NPY(16–36) produced a similar degree of inhibition, irrespective of whether nicotine or an equipotent concentration of acetylcholine was used to evoke IACh. NPY(16–36) failed to alter voltage-dependent inward or outward currents. Intracellular cAMP, and extracellular dibutyryl-cAMP, produced a slowly developing increase in IACh. Intracellular cAMP, extracellular 8-Br-cAMP or dibutyryl-cAMP, and an inhibitor of cyclic nucleotide phosphodiesterases 3-isobutyl-l-methylxanthine (IBMX), decreased the inhibitory effect of NPY(16–36) on lACh. Although the intracellular application of the cAMP-dependent protein kinase A inhibitor [PKI(14–24)amide] alone did not alter IACh, it potentiated the effect of NPY(16–36) in interaction experiments. While the NPY(16–36)-induced inhibition of IACh was reversed on washout of the peptide, the slightly shorter C-terminal fragment NPY(18–36) caused a long-lasting depression of both IAch and catecholamine secretion evoked by nicotine. This depression was smaller in the presence of extracellular 8-Br-cAMP than in its absence. NPY(18–36) did not alter the secretory activity induced by a high concentration of potassium. It appears that, by activating Y3-receptors, NPY inhibits nAChR-current and the resulting secretion of catecholamines from bovine chromaffin cells. This process may involve a G protein-mediated decrease in intracellular cAMP with a subsequent decrease in the degree of phosphorylation of the nAChR-channel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169073
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    Paper (German National Licenses)
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  • 10
    Electronic Resource
    Electronic Resource
    Secondary structural changes of chymotrypsinogen A, alpha-chymotrypsin, and the isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245 in sodium dodecyl sulfate, urea and guanidine hydrochloride (1990)
    Springer
    Colloid & polymer science 268 (1990), S. 612-617 
    Details
    ISSN: 1435-1536
    Keywords: Chymotrypsinogen ; chymotrypsin fragments ; CD ; secondary structure ; sodiumdodecylsulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Secondary structural changes of chymotrypsinogen A,α-chymotrypsin, and their isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245were examined in aqueous solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride (residue numbers from chymotrypsinogen). After the fragmentation by the cleavage of disulfide bridges inα-chymotrypsin, the helical structure was formed in the isolated polypeptide 16–146 where the helical segments do not exist in the protein state. The polypeptide 149–245, where the helical segments of the parent protein are originally located, contained no helices. The polypeptide 1–13 was almost disordered. The three polypeptides, chymotrypsinogen,α-chymotrypsin and the polypeptide 16–146, clearly showed differences in the stabilities of helical structures in solutions of urea and guanidine hydrochloride. The addition of SDS accelerated the formation of helical structures in each polypeptide except for 1–13.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01410401
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