<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Katre, Uma V.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, S. M.</style></author><author><style face="normal" font="default" size="100%">Bhagyawant, S. S.</style></author><author><style face="normal" font="default" size="100%">Deshpande, U. D.</style></author><author><style face="normal" font="default" size="100%">Khan, Mohammad Islam</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Crystallization and preliminary x-ray characterization of a lectin from Cicer arietinum (chickpea)</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallographica Section F-Structural Biology and Crystallization Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">BLACKWELL PUBLISHING</style></publisher><pub-location><style face="normal" font="default" size="100%">9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">61</style></volume><pages><style face="normal" font="default" size="100%">141-143</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">0.647</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Balakrishnan, H.</style></author><author><style face="normal" font="default" size="100%">Satyanarayana, L.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, S. M.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp (NCL 87-6-10)</style></title><secondary-title><style face="normal" font="default" size="100%">Enzyme and Microbial Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">active-site residues</style></keyword><keyword><style  face="normal" font="default" size="100%">alkaline xylanase</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemical modification</style></keyword><keyword><style  face="normal" font="default" size="100%">three-dimensional structure</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE INC</style></publisher><pub-location><style face="normal" font="default" size="100%">360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA</style></pub-location><volume><style face="normal" font="default" size="100%">39</style></volume><pages><style face="normal" font="default" size="100%">67-73</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Structural studies and residue modification using group specific reagents were used to ascertain the role of different functional groups in xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). Treatment with N-bromosuccinimide resulted in fast enzyme inactivation. Reaction with Woodward's reagent K resulted in initial fast followed by slower inactivation. In both cases enzyme was protected against inactivation by the substrate, xylan. The reaction of the enzyme with phenylglyoxal has revealed one essential arginine residue at the active site. The three-dimensional structural analysis of the xylanase at 2.8 angstrom resolution also implicates involvement of Trp, and Arg residues and carboxylate groups in the binding of substrate and in the catalysis of xylanase. (c) 2005 Published by Elsevier Inc.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.624</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shashidhara, K. S.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, S. M.</style></author><author><style face="normal" font="default" size="100%">Khan, Mohammad Islam</style></author><author><style face="normal" font="default" size="100%">Bharadwaj, Kishor Chandra</style></author><author><style face="normal" font="default" size="100%">Pandey, G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Interaction of alpha-mannosidase from aspergillus fischeri with glycosidase inhibitors, metal ions and group specific reagents</style></title><secondary-title><style face="normal" font="default" size="100%">Research Journal of Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">active-site</style></keyword><keyword><style  face="normal" font="default" size="100%">alpha-Mannosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemical modification</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosidase inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">metal ions</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">RESEARCH JOURNAL BIOTECHNOLOGY</style></publisher><pub-location><style face="normal" font="default" size="100%">SECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">39-48</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;As an initial step towards using alpha-mannosidase as a target against anticancer drugs, inhibition studies of a model enzyme, class II alpha-mannosidase from Aspergillus fischeri in presence of polyhydroxy piperidine derived glycosidase inhibitors, metal ions and amino acid specific reagents were carried out to reveal the sensitivity of the enzyme. Three of the derivatives (Compound 20, 32 and 39)(11) showed competitive inhibition (K(i) =45, 48 and 235 mu M) and the binding of the inhibitors to the enzyme was entropically driven. Among the metal ions checked, Cu(++) (K(i) = 21nm) and Se(++) ions (K(i) = 32 mu M) showed noncompetitive and Co(++) (K(i) = 1.195 mM) showed competitive inhibition of the enzyme activity with insignificant change in the secondary structure of the protein. The above studies exhibit the Potential of the enzyme in studying anticancer drugs. Treatment of the enzyme with group specific reagents showed the presence of carboxylate, Arg and Cys at the active site. Substrate protection studies and kinetics of the modified enzyme confirmed the above results. Trp and His at the active site were observed to be in proximity.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom3><style face="normal" font="default" size="100%">Indian</style></custom3><custom4><style face="normal" font="default" size="100%">0.284</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Elangovan, M.</style></author><author><style face="normal" font="default" size="100%">Dholakia, Bhushan B.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, S. M.</style></author><author><style face="normal" font="default" size="100%">Gupta, V. S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Differential accumulation of gliadin proteins in wheat grain of RILs grown at two different agroclimatic conditions and their effect on loaf volume</style></title><secondary-title><style face="normal" font="default" size="100%">Australian Journal of Crop Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">loaf volume (Lv)</style></keyword><keyword><style  face="normal" font="default" size="100%">RP-HPLC</style></keyword><keyword><style  face="normal" font="default" size="100%">Wheat protein</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">SOUTHERN CROSS PUBL</style></publisher><pub-location><style face="normal" font="default" size="100%">8 91-93 MCKENZIE ST, LISMORE, NSW 2480, AUSTRALIA</style></pub-location><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">63-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The end use of wheat depends on the quality and quantity of protein accumulated in the grain during the grain filling stage. Gliadin families of proteins are proved to affect the bread making quality (BMQ) by affecting the rheology and functionality of dough. The gliadin accumulation was analysed using Indian genotypes grown in two diverse agro climatic zones. About 16 RILs along with their parents HI977 and HD2329 revealed significant difference in accumulation of all gliadin fractions. High accumulation of alpha and beta gliadin with low level of gamma gliadin was observed for Kota as compared to Pune location. However, this significant difference in gliadin accumulation due to environment, did not affect the loaf volume performance of the RILs at statistically significant level.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">0.899</style></custom4></record></records></xml>