Denaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride
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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...
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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...
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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...
متن کاملReversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation.
The pH-dependent transitions and the thermal unfolding of defatted human serum albumin in 0.2 M KC1 as followed by polarimetry at 233 nm are found to be independent processes. The apparent net loss of structure (01 helix) in the unfolding between pH ‘7 and 9 is 2.5%, in the N-F transformation it is 8% and in the acid expansion 1%. The two last mentioned transitions seem to be independent of eac...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43163-3