TY - JOUR
T1 - The effect of antimycin A on mouse liver inner mitochondrial membrane channel activity
AU - Campo, Maria Luisa
AU - Kinnally, Kathleen W.
AU - Tedeschi, Henry
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1992/4/25
Y1 - 1992/4/25
N2 - In a patch-clamp study, we found antimycin A in low (1-2) μM concentrations decreased the open probability of the multiple conductance channel activity and the ∼110 picosiemens channel of the inner mitochondrial membrane (for a review of mitochondrial channels see Kinnally, K. W., Antonenko, Yu. N., and Zorov, D. B. (1992) J. Bioenerg. Biomembr. 24, 99-110). Higher antimycin A concentrations (e.g. 10 μM) facilitated multiple conductance channel opening. These effects were reversible, and the binding site(s) are probably distinct from those responsible for the inhibition of the electron transport chain, since the latter are virtually irreversible. A model with two closed and two open states is presented for the ∼110-picosiemens activity.
AB - In a patch-clamp study, we found antimycin A in low (1-2) μM concentrations decreased the open probability of the multiple conductance channel activity and the ∼110 picosiemens channel of the inner mitochondrial membrane (for a review of mitochondrial channels see Kinnally, K. W., Antonenko, Yu. N., and Zorov, D. B. (1992) J. Bioenerg. Biomembr. 24, 99-110). Higher antimycin A concentrations (e.g. 10 μM) facilitated multiple conductance channel opening. These effects were reversible, and the binding site(s) are probably distinct from those responsible for the inhibition of the electron transport chain, since the latter are virtually irreversible. A model with two closed and two open states is presented for the ∼110-picosiemens activity.
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M3 - Article
C2 - 1569069
AN - SCOPUS:0026646597
SN - 0021-9258
VL - 267
SP - 8123
EP - 8127
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 12
ER -