<?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%">Dutta, Somenath</style></author><author><style face="normal" font="default" size="100%">De, U. S.</style></author><author><style face="normal" font="default" size="100%">Devi, Sunitha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Diagnostic study on the energetics aspects of hiatus in the advance of southwest monsoon</style></title><secondary-title><style face="normal" font="default" size="100%">Mausam</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Energetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Hiatus</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%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">INDIA METEOROLOGICAL DEPT</style></publisher><pub-location><style face="normal" font="default" size="100%">MAUSAM BHAWAN, LODI RD, NEW DELHI, 110 003, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">60</style></volume><pages><style face="normal" font="default" size="100%">427-436</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Advance of southwest monsoon, after its onset, often gets stalled for a week or more causing concern to the farmers and other community whose activities are weather dependent. The present study on the energetics aspect of hiatus in the advance of southwest monsoon over India aims at understanding the dynamical reasons for this. Nine cases of hiatus of duration more than 10 days during 1982-2006 have been selected. For each hiatus case, different energy terms, their generation and conversion among different terms have been computed during the hiatus period and also during the pre-hiatus pentad over a limited region between 65 degrees E to 90 degrees E, 5 degrees N to 30 degrees N. These computations are based on NCEP 2.5 degrees x 2.5 degrees re-analysed daily composite data during different hiatus period and during corresponding pre-hiatus pentad. From this study it is found that : (i) In most of the cases there is a reduction in the generation of zonal available potential energy [G(A(Z))] during hiatus period compared to pre-hiatus pentad. (ii) Drop in the conversion from zonal available potential energy to zonal kinetic energy [C(A(Z), K(Z))] during hiatus period has been observed in most of the cases. (iii) In most of the cases there is a reduction in zonal kinetic energy (K(Z)) and in eddy kinetic energy (K(E)) during hiatus period compared to pre-hiatus pentad.&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%">0.110</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%">Kumar, Avinash</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Jack bean alpha-mannosidase (Jb alpha-man): tolerance to alkali, chelating and reducing agents and energetics of catalysis and inhibition</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkali tolerance</style></keyword><keyword><style  face="normal" font="default" size="100%">alpha-Mannosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">beta-Mercaptoethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Energetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Inhibition</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloenzyme</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">49</style></volume><pages><style face="normal" font="default" size="100%">1066-1071</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Investigations of the catalytic and structural transitions of jack bean alpha-mannosidase (Jb alpha-man) are described in the present paper. The enzyme was maximally stable at pH 5.0; however, when incubated in the pH range of 11.0-12.0, showed 1.3 times higher activity and also stability for longer time. The free amino group at or near the active site was probably involved in the stability and activation mechanism. The active site is constituted by the association of two unidentical subunits connected by disulfide linkages. The metalloenzyme has Zn(2+) ions tightly bound and chelation reduces the thermal stability of the protein. Energetics of catalysis and thermodynamics of inhibition of the enzyme were also carried out. (C) 2011 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><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%">3.09</style></custom4></record></records></xml>