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L-Arginine increases the solubility of unfolded species of hen egg white lysozyme

¹ School of Biotechnology, Banaras Hindu University, Varanasi-221005, India² Institut für Biotechnologie, Martin-Luther-Universität Halle/Wittenberg, 06120 Halle (Saale), Germany

(RECEIVED August 31, 2004; FINAL REVISION November 27, 2004; ACCEPTED December 3, 2004)

L-Arginine (L-Arg) has been widely used as an enhancer of protein renaturation. The mechanism behind its action is still not fully understood. Using hen egg white lysozyme as a model protein, we present data that clearly demonstrate the suppression of the aggregation of denatured protein by L-Arg. By chemical modification of free cysteines, a series of unfolded lysozyme species were obtained that served as models for unfolded and intermediate states during the process of oxidative refolding. An increased equilibrium solubility of unfolded species and intermediates in the presence of L-Arg seems to be its major mechanism of action.

Keywords: refolding; aggregation; L-arginine; lysozyme

Abbreviations: DTT, dithiothreitol • DSC, differential scanning calorimetry • GSH, reduced glutathione • GSSG, oxidized glutathione • GuHCl, guanidinium chloride • L-Arg, L-arginine • L-ArgHCl, L-arginine monohydrochloride • [x], concentration of compound x

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041085005.

Reprint requests to: Christian Lange, Institut für Biotechnologie, Martin-Luther-Universität Halle/Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle (Saale), Germany; e-mail: christian.lange{at}biochemtech.uni-halle.de; fax: +49-345-55-27013.

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