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  • 1
    Electronic Resource
    Electronic Resource
    Differential sensitivity of cardiac K(ATP) + channels to guanine nucleotides — evidence for a heterogeneous channel population (1992)
    Springer
    European biophysics journal 21 (1992), S. 299-302 
    Details
    ISSN: 1432-1017
    Keywords: Cardiac K(ATP) + channels ; GTP ; GDP ; Heart muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract In cell-free patches from cultured neonatal rat cardiocytes, the cytosolic presence of GTP-γ-S (100 µmol/l) or GDP-\-S (100 µmol/1) activated K(ATP) + channels. GTP-γ-S required cytosolic Mg++, suggesting that an activated G-protein causes the increase in open probability. The great variations of the channel response to GTP-γ-S and GDP-\-S indicates that cardiac K(ATP) + channels represent a heterogeneous family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00185124
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Single cardiac outwardly rectifying K+ channels modulated by protein kinase A and a G-protein (1991)
    Springer
    European biophysics journal 20 (1991), S. 281-286 
    Details
    ISSN: 1432-1017
    Keywords: Cardiac K+ channels ; Phosphorylation ; GTP ; GDP ; Neonatal rat heart myocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Elementary K+ currents were recorded at 19 °C in cell-attached and in inside-out patches excised from neonatal rat heart myocytes. An outwardly rectifying K+ channel which prevented Na+ ions from permeating could be detected in about 10% of the patches attaining (at 5 mmol/l external K+ and between − 20 mV and + 20 mV) a unitary conductance of 66 +- 3.9 pS. K (outw.-rect.) + channels have one open and at least two closed states. Open probability and τopen rose steeply on shifting the membrane potential in the positive direction, thereby tending to saturate. Open probability (at −7 mV) was as low as 3 ± 1% but increased several-fold on exposing the cytoplasmic surface to Mg-ATP (100 μmol/l) without a concomitant change of τopen. No channel activation occurred in response to ATP in the absence of cytoplasmic Mg−+. The cytoplasmic administration of the catalytic subunit of protein kinase A (120–150 μ/ml) or GTP-γ-S (100 μmol/l) caused a similar channel activation. GDP-β-S (100 μmol/l) was also tested and found to be ineffective in this respect. This suggests that cardiac K (outw.-rect.) + channels are metabolically modulated by both cAMP-dependent phosphorylation and a G-protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00450563
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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