J. Biol. Chem., Vol. 260, Issue 3, 1374-1377, 02, 1985
Functionally distinct beta subunits in F1-adenosinetriphosphatase
JH Wang
A method has been developed for the effective inactivation of bovine heart
mitochondrial F1-ATPase (MF1) by partially dissociating its subunits with 3
M LiCl at 0 degree C and for the subsequent partial restoration of its
ATPase activity by making the subunits reassociate upon the removal of LiCl
by centrifugal gel filtration at room temperature through Sephadex G-25-80
which has been pre-equilibrated with buffer containing 3 mM ATP. When
covalently labeled MF1 with approximately one
7-[4-nitro-2,1,3-benzoxadiazole] label/MF1 was subjected to this type of
partial dissociation-reassociation treatment, its ATPase activity could be
increased from 1.48 to 18.0 mumol of ATP min-1 mg-1 without losing the
covalent label. The experimental results are incompatible with models for
F1-ATPase with either 3 or 2 equivalent alternating catalytic sites, but
are consistent with the model with 1 active catalytic site and 2
interacting regulatory sites.
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