The transition curves of soybean glycinin egg lysozyme, bovine serum albumin (BSA) denaturation under the action of increasing urea concentration were monitored by determination of the increase in rate constants of cooperative enzymatic proteolysis. The results were compared with those obtained using intrinsic fluorescence and the number of accessible tyrosine. It was shown that the determination of the changes of proteolysis rate permits to disclose conformation changes not detected by other methods.
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