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, 2, 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 2, p.p. 59 63</center></b> <br> <div> <p><b><font size=+2> Regulation of Ca<SUP>2+</SUP>,Mg<SUP>2+</SUP>-ATPase activity by inositol-specific lectin isolated from synaptic vesicle membranes </font></b></p> <p> <b> Nana Koshoridze,* Nino Surgulagze and Ketevan Menabde </b> <br> <br> <i> Department of Biology, I. Javakhishvili State University, 2 University St, 0128 Tbilisi, Georgia </i></p> <P align=justify> The action of the inositol-specific BVL-I lectin isolated from brain synaptic vesicles on the Ca<SUP>2+</SUP>,Mg<SUP>2+</SUP>-ATPase activity of the neural actomyosin-like contractile protein has been investi¬gated. We found that Ca<SUP>2+</SUP>,Mg<SUP>2+</SUP>-ATPase activity occurred within the range 0.004 0.5 mM of calcium, maximal activity was observed at a concentration of 0.5 mM Ca<SUP>2+</SUP>, while further increase of concentration (2.5 10 mM) reduced the activity. In the presence of different concentrations of lectin (2 and 20 ¼g/mL), the character of the activity shows no significant change, although the enzyme s activity is considerably increased compared with the control experiments. The data suggest that BVL-I lectin could participate in the various transport processes, including translocation of synaptic vesicle and exocytosis of neurotransmitters </p> <b>Keywords: </b> actomyosin-like protein, Ca<SUP>2+</SUP>,Mg<SUP>2+</SUP>-ATPase, lectin, synaptic vesicles </p> <br> </div> <p></p> <center><p><i><font size=-1><a href="jbpc20707.html">back to contents</a></font></i></p></center> </body> </html>