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  • Electronic Resource  (2)
  • 2005-2009
  • 1990-1994  (1)
  • 1970-1974  (1)
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  • 1900-1904
  • Chemistry  (1)
  • Ionic currents  (1)
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  • Electronic Resource  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 422 (1993), S. 325-331 
    ISSN: 1432-2013
    Keywords: Myocyte ; Voltage clamp ; Ionic currents ; Oximes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Exposure of isolated guinea-pig ventricular myocytes to the uncharged oximes 2,3 butanedionemonoxine (BDM) and norPAM (but not by the charged PAM) results in a dose-dependent reduction of the duration of the action potential. The nifedipine-sensitive Ca current is fully inhibited by BDM (IC505.8±0.4 mM) and nor PAM but is little affected by PAM. This inhibition is unaltered by the presence of BAY K 8644 but is antagonized by isoprenaline. The effect of isoprenaline is more pronounced when the solution in the patch pipette contains the non-hydrolysable analogue of adenosine 5′-triphosphate, ATPγS (the IC50 is increased to 44.0±5.2 mM). A hastening of the inactivation of the L-type Ca current persists when either 10 mM 1,2-bis(2-aminophenoxy)-ethane-N, N, N′, N-tetraacetic acid (BAPTA) or 3 mM ATPγS is present in the pipette solution or when BAY K 8644 or isoprenaline are present in the bathing fluid. These results suggest that the inhibition of the Ca current is due to the phosphatase-like activity of the oximes but differs in some respects from previous work where a reduced level of phosphorylation is achieved by the introduction of protein kinase inhibitors or protein phosphatases into the sarcoplasm in guinea-pig myocytes. These differences could be explained if Ca channel availability is regulated by at least two sites of cAMP-dependent phosphorylation with oximes able to rapidly dephosphorylate both sites, while one of these sites is not readily dephosphorylated by the endogenous phosphatases.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 9 (1970), S. 445-457 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The change in apparent molal volume φ of DNA on thermal denaturation in carbonate buffer at pH 11.0 has been determined by the dilatometric method. It was found that φ increases sigmoidally during the helix-coil transition. Several methods, including a colorimetric technique that closely simulates the conditions used in the dilatometric experiments, were employed to estimate the protons lost by the DNA during the transition. These measurements indicated that the extent of the proton loss depends on the counterion present, increasing in the order Li+ 〈 Na+ 〈 K+ 〈 Cs+. The major part of the volume changes observed during the denaturation is due to the volume changes expected to accompany the transfer of protons from the bases guanine and thym ne to carbonate ions. As has been previously reported for the denaturation of DNA at neutral pH, the volume change directly due to the change in shape of the polymer molecules is so small as to be experimentally undetectable.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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