ÿþ<html> <head> <meta http-equiv="Content-Type" content="text/html; charset=windows-1251"> <meta name="Author" content> <meta name="Description" content="Contents and Abstracts of Journal Voprosy Meditsinskoi Khimii (Biomedical Chemistry)."> <meta name="KeyWords" content="polyamine metabolism, inhibitors of polyamine biosynthesis, ornitine decarboxylase,polyamine oxidase"> <meta name="GENERATOR" content="Microsoft FrontPage 6.0"> <title>Russian Journal: Biomeditsinskaya Khimiya (Biomedical Chemistry) Contents &amp; Abstracts</title> </head> <body background="../../4506/grayt.gif" bgcolor="#FFFFFF" text="#000000" link="#0000FF" vlink="#800080" alink="#0000FF"> <table border="0" cellpadding="0" cellspacing="0" width="100%"> <tr> <td valign="top"> <img alt="eng1.gif (176 bytes)" border="0" src="../pic/eng2.gif" width="39" height="16"><a href="../5301r/8r.htm"><img border="0" src="../pic/rus1.gif" width="39" height="16"></a></td> <td valign="top"><p align="center"><font size="5" face="Times New Roman CE"><b>Russian Journal</b></font></td> <td align="right" valign="top"><font face="Times New Roman CE">ISSN 0042-8809</font></td> </tr> </table> <div align="center"><center> <table border="0" cellpadding="0" cellspacing="0" width="100%"> <tr> <td valign="top"><font size="5" face="Times New Roman CE"><b>Biomeditsinskaya Khimiya</b></font></td> <td valign="top"><p align="right"><font size="5" face="Times New Roman CE"><b>Biomedical Chemistry</b></font><font face="Times New Roman CE"> </font></td> </tr> </table> </center></div> <hr> <p align="center"><font face="Times New Roman CE"> <a style="font-family: Arial; font-size: 10pt; font-weight: bold; color: #003399; text-decoration: none blink" href="../../default.htm">Home</a>&nbsp; </font><font face="Times New Roman">&#1472;&nbsp; <a style="font-family: Arial; font-size: 10pt; color: #003399; font-weight: bold; text-decoration: none" href="../../board.htm">Editorial Board</a> &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../council.htm">International Advisory Board</a>&nbsp; &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../aim.htm">Aim and Scope</a> &#1472;&nbsp;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../content.htm">Contents and Abstracts</a>&nbsp; &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../information.htm">Information for Authors</a> &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../subscribe.htm">Subscribe Now</a></font></p> <hr> <p><b>Issue: <br> </b>Volume 53, issue 1</p> <p><strong> Title:</strong> INFLUENCE OF ZN(II) AND MN(II) ON CATALYTIC ACTIVITY OF ASPARTIC PROTEINASES OF CANDIDA ALBICANS </p> <p class="MsoNormal"><strong> Authors: </strong> M.P. Kutyreva<sup>1</sup>, R.R. Galimzanova<sup>1</sup>, N.A. Ulahovich<sup>1</sup>, N.I. Glushko<sup>2</sup> </p> <p><b>Address: </b></p> <sup>1</sup>Kazan State University, ul. Kremlevskaya, 18, Kazan, 420008 Russia, tel.: (843)232-03-15; e-mail: <a href=mailto:MariannaKutyreva@ksu.ru>MariannaKutyreva@ksu.ru</a><br> <sup>2</sup>Kazan Research Institute of Epidemiology and Microbiology, ul. Bolshaya Krasnaya, 67, Kazan, 420008 Russia; tel.: (843)236-56-59 </p> <p><b>Abstract:</b> <p> The interaction of secreted aspartic proteinases Candida <i>albicans</i> (SAP C. <i>albicans</i>) with ZnCl<sub>2</sub> and MnCl<sub>2</sub> was studied. Logarithms of stability constant from the data of electronic spectroscopy were calculated: lg² = 4,73±0,20 for the complex [SAP C. <i>albicans</i> - Zn(II)] and lg² = 7,02±0,20 for the complex [SAP C. <i>albicans</i> - Mn(II)]. The composition and maximum accumulation of complexes in solution were calculated. The optimal conditions of hydrolysis of the substrate, HAS (human serum albumin) in the presence of proteinases were determined: [HSA]=0.004 g/ml, [SAP]=2.33 mM, pH=4.5, the time of incubation of 25 min. The activity SAP C. <i>albicans</i> in the presence of ZnCl<sub>2</sub> and MnCl<sub>2</sub> in different concentrations in optimal conditions of enzymic hydrolysis was estimated. For the first time the activating action of ZnCl<sub>2</sub> on catalytic activity of proteinase in concentration 5×10<sup>-7</sup> mol/l was discovered. The maximal rate of enzymic reaction (V<sub>m</sub>), the Michaelis constant (K<sub>m</sub>) and constants of effects in presence and absence as the effector of ZnCl<sub>2</sub> were calculated. The estimation of albuminatic activity of C. <i>albicans</i> infections family in different diseases localization in the presence and the absence as the effector of ZnCl<sub>2</sub> was evaluated. <p><b>Key words:</b> proteinases of <i>Candida albicans</i>, enzymic catalysts, effectors, kinetic parameters. </span></p> <b style="mso-bidi-font-weight:normal"> <hr> <p align="center"></b>[<a href="http://www.ibmc.msk.ru/pbmc/2007/5301/vol53is1.htm#8">Back</a>]<b style="mso-bidi-font-weight:normal"><b style="mso-bidi-font-weight:normal"></p> </b></b></font> </body> </html>