J. Biol. Chem., Vol. 261, Issue 17, 7807-7810, 06, 1986
Mitochondrial H+-ATPase activation by an amine oxide detergent
N Vazquez-Laslop and G Dreyfus
Lauryl dimethylamine oxide activates ATP hydrolysis by the mitochondrial
H+-ATPase. Activation is observed in systems with a high content of
inhibitor protein as described by Pullman and Monroy (Pullman, M.E., and
Monroy, G.C. (1963) J. Biol. Chem. 238, 3762-3769), i.e. Mg-ATP
submitochondrial particles and a Triton X-100-solubilized H+-ATPase from
the same particles. Detergent activation of ATP hydrolysis is also present
in inhibitor-reconstituted systems, i.e. submitochondrial particles, Triton
extracts, and soluble F1-ATPase. In submitochondrial particles depleted of
inhibitor protein, lauryl dimethylamine oxide induced a biphasic response
which is characterized by a drop-in activity induced by relatively low
concentrations of LDAO; at higher concentrations the detergent activates to
an extent never greater than the initial activity. In inhibitor
protein-depleted oligomycin-sensitive Triton extracts, lauryl dimethylamine
oxide stimulates ATP hydrolysis to very high values (30 mumol min-1 mg-1).
These findings suggest that in addition to the inhibitor protein ATP
hydrolysis is controlled by other subunit interactions.
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