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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 112 (1989), S. 91-96 
    ISSN: 1432-1424
    Keywords: Paramecium ; patch clamp ; K channel ; Ca2+ dependence ; proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effects of proteolysis on a hyperpolarization- and Ca2+-dependent K channel from the surface membrane ofParamecium tetraurelia were examined in the inside-out excised patch mode. Treatment with trypsin, pronase or thermolysin removed the Ca2+-dependence of the channel activation, yielding an increase in channel activity greater than 2.5-fold at all Ca2+ concentrations between 10−4 and 10−8 m. Thermolysin addition-ally removed the voltage dependence of channel opening and gave the most activation among the three proteases tested. Proteolysis did not affect the single-channel conductance. In an analogy to the mechanism of activation of many Ca2+-dependent enzymes it is suggested that thisParamecium channel has a cytoplasmic inhibitory domain which can be removed by proteolysis, and that the physiological activation by Ca2+ is due to a temporary removal of this inhibition. Moreover, these findings indicate structural differences between depolarization-, Ca2+-dependent K channels (BK channels) and the hyperpolarization-, Ca2+-dependent K channels inParamecium.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 115 (1990), S. 41-50 
    ISSN: 1432-1424
    Keywords: inward rectification ; voltage-dependent K+ current ; Ca2+-dependent K+ current ; Paramecium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Hyperpolarization of voltage-clampedParamecium tetraurelia in K+ solutions elicits a complex of Ca2+ and K+ currents. The tail current that accompanies a return to holding potential (−40 mV) contains two K+ components. The tail current elicited by a step to −110 mV of ≥50-msec duration contains fast-decaying (τ≈3.5 msec) and slow-decaying (τ≈20 msec) components. The reversal potential of both components shifts by 55–57 mV/10-fold change in external [K+], suggesting that they represent pure K+ currents. The dependence of the relative amplitudes of the two tail currents on duration of hyperpolarization suggests that the slow K+ current activates slowly and is sustained, whereas the fast current activates rapidly during hyperpolarization and then rapidly inactivates. Iontophoretic injection of a Ca2+ chelator, EGTA, specifically reduces slow tail-current amplitude without affecting the fast tail component. Both K+ currents are inhibited by extracellular TEA+ in a concentration-dependent, noncooperative manner, whereas the fast K+ current alone is inhibited by 0.7mm quinidine.
    Type of Medium: Electronic Resource
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