Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation.

Abstract

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… (More)

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