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Fig. 9. Structural unfolding and enzymatic inhibition by urea of foot muscle
Na+/K+-ATPase from active and estivating snails. Enzyme
extracts were denatured overnight with different concentrations of urea and
then either treated with thermolysin or assayed under optimal conditions. (A)
Mean relative Na+/K+-ATPase protein remaining (as
quantified from band intensities on western blots) after overnight incubation
with urea and subsequent proteolysis with thermolysin; values are means
± s.e.m., N=3 independent trials. (B) Mean relative activity
of foot muscle Na+/K+-ATPase from active and estivating
snails as a function of overnight incubation with different concentrations of
urea; values are means ± s.e.m., N=3.
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