Mercurials selectively inhibited 414 ATPase (EC Inhibition of the soluble ATPase (BF) was greater than for the membrane-bound enzyme. The titration of 4 SH groups per mol BF with 0.05 mM--chloromercuri[C]benzoate showed a good dose-response curve for the inhibition of basal ATPase but not for the trypsin-stimulated activity. Accessible SH groups did not seem to be related to the active site of the enzyme. Mercurials appeared to affect ATPase by inducing a molecular change in the holo-enzyme, followed by dissociation. One to two SH groups with different degrees of accessibility were located in the α. and γ subunits of ATPase (BF) but only one was located in the β subunit, irrespective of the concentration of -chloromercuribenzoic acid, suggesting a structural role for SH groups in BF


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