Activation of bovine muscle carbonic anhydrase by modification of thiol groups
نویسندگان
چکیده
منابع مشابه
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...
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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...
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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 ...
متن کاملEffects of surface charge on denaturation of bovine carbonic anhydrase.
This work compares the denaturation of two proteins-bovine carbonic anhydrase II (BCA) and its derivative with all lysine groups acetylated (BCA-Ac(18))-by urea, guanidinium chloride (GuHCl), heat, and sodium dodecyl sulfate (SDS). It demonstrates that increasing the net negative charge of the protein by acetylation of lysines reduces its stability to urea, GuHCl, and heat, but increases its ki...
متن کاملCombination of bovine carbonic anhydrase with a fluorescent sulfonamide.
Bovine erythrocyte carbonic anhydrase forms a highly fluorescent complex with 5-dimethylaminonapbthalene-lsulfonamide (DNSA). The binding, studied either by enhancement of ligand fluorescence or by the quenching of protein ultraviolet fluorescence, shows that only 1 mole of DNSA is bound per mole of protein; the dissociation constant at pH 7.4 is 2.5 X lo-’ M. The fluorescence of free DNSA in w...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1986
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1986.tb09597.x