Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...