Collect. Czech. Chem. Commun. 1989, 54, 536-543

Polarographic studies on renaturation of urea-denatured human serum albumin

Josef Chmelíka, Pavel Anzenbacherb and Vítěz Kalousc

a Institute of Analytical Chemistry, Czechoslovak Academy of Sciences, 611 42 Brno
b Department of Biochemistry, Charles University, 128 40 Prague 2
c Department of Physical Chemistry, Charles University, 128 40 Prague 2


The renaturation of the two main components of human serum albumin, i.e. of mercaptalbumin and nonmercaptalbumin, was studied polarographically. It has been demonstrated that renaturation of both proteins after 1-min denaturation in 8M urea is reversible. By contrast, renaturation after 200 min denaturation in 8M urea is an irreversible process; the characteristics of renatured mercaptalbumin differ more from the properties of the native protein than the characteristics of nonmercaptalbumin. The studies of the kinetics of renaturation of both proteins have shown that the renaturation can be represented by a two-state model. This means that the existence of stable intermediary products during the renaturation process was not determined polarographically.