þÿ<!DOCTYPE HTML PUBLIC "-//W3C//DTD HTML 4.0 Transitional//EN"> <HTML> <head> <meta http-equiv="Content-Type" content="text/html; charset=utf-8"> <title>JBPC Vol. 7, 3, 2007 ABSTRACT </title> </head> <body link="#0000FF"><center><h1><font color="#006600">The Journal of Biological Physics and Chemistry</font></h1></center> <p></p><p></p> <b><center>2007<p>Volume 7, Number 3, p.p. 97 102</center></b> <br> <div> <p><b><font size=+2> Calorimetric study of bovine and human serum albumins and their complexes with bilirubin </font></b></p> <p> <b> M. Khvedelidze,* T. Mdzinrashvili, A. Trapaidze, E. Kortkhondjia and G. Mrevlishvili </b> <br> <br> <i> I. Javakhishvili State University, 3 Chavchavdze Ave, 0128 Tbilisi, Georgia<br> </i></p> <P align=justify> Thermodynamic properties of bovine and human serum albumin solutions were studied using a differential scanning microcalorimeter, i.e. the dependence of partial heat capacity on temperature was determined. The predenaturation and main changes of the protein s partial heat capacity during thermal denaturation were obtained. Deconvolution of the partial heat capacity function indicates that the process of denaturation consists of three transitions; each of them corresponds to the melting of three different structural domains. Analysis of the microcalorimetric melting curves of the albumin-bilirubin complex together with the thermodynamic parameters of the domains show that the bilirubin binding is localized in domain II of the albumin molecule. </p> <b>Keywords: </b> bilirubin, calorimetry, human and bovine serum albumin, ligand connexion, protein denaturation, thermodynamics </p> <br> </div> <p></p> <center><p><i><font size=-1><a href="jbpc30707.html">back to contents</a></font></i></p></center> </body> </html>