Activation and inhibition of bovine carbonic anhydrase III by dianions.

Denaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride

The denaturation and renaturation of bovine carbonic anhydrase B is a thermodynamically reversible process, uncomplicated by aggregation or disuhide bond formation. The reaction is less cooperative than is the unfolding and refolding of most globular proteins, in that distinct successive stages can be observed both in equilibrium and kinetic measurements. This enzyme is therefore ideally suited...

Irreversible inactivation of bovine carbonic anhydrase B by bromoacetazolamide.

Bromoacetazolamide effects rather quickly a partial, and more slowly an almost complete, irreversible inactivation of bovine carbonic anhydrase B (EC 4.2.1.1). Under identical conditions, the enzyme is not inactivated by bromoacetic acid or iodoacetamide, nor does it react significantly with these compounds. The zinc-free enzyme does not undergo irreversible binding with W-bromoacetazolamide an...

Hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle.

We report three experiments which show that the hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle occurs at a site on the enzyme different than the active site for CO2 hydration. This is in contrast with isozymes I and II of carbonic anhydrase for which the sites of 4-nitrophenyl acetate hydrolysis and CO2 hydration are the same. The pH profile ...

Novel inhibition of carbonic anhydrase isozymes I, II and III by carbamoyl phosphate.

Carbamoyl phosphate has been shown to inhibit carbonic anhydrase (CA) isozymes CA I, CA II and CA III. This physiologically important molecule is the most potent, naturally occurring inhibitor of carbonic anhydrase yet found. It is also unique, among carbonic anhydrase inhibitors discovered hitherto, in that it inhibits the 3 isozymes with equal effect, despite their strikingly different proper...

Carbonic anhydrase: chemistry, physiology, and inhibition.