Acid Denaturation of Human Carbonic Anhydrase B. A Fluorimetric Kinetic Study
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...
متن کاملDenaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions.
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...
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 کاملHuman carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer.
The residue phenylalanine 198 (Phe 198) is a prominent cause of the lower activity of human carbonic anhydrase III (HCA III) compared with HCA II and other isozymes which have leucine at this site. We report the crystal structures of HCA III and the site-directed mutant F198L HCA III, both at 2.1 A resolution, and the enhancement of catalytic activity by exogenous proton donors containing imida...
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The carbonic anhydrase activity of human platelets was investigated by measuring the kinetics of CO2 hydration in supernatants of platelet lysates by using a pH stopped-flow apparatus. An average carbonic anhydrase concentration of 2.1 microM was determined for pellets of human platelets. Analysis of the kinetic properties of this carbonic anhydrase yielded a Km value of 1.0 mM, a catalytic-cen...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03480.x