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In vitro stability of various enzymes by proline from H2O2 mediated oxidative damage

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Title In vitro stability of various enzymes by proline from H2O2 mediated oxidative damage
 
Creator Dalal, Vijay Kumar
Biswal, Ajay K
Patel, Dhaval
Subramanyam, Rajagopal
Raghavendra, Agepati S
 
Subject ANS
CD
Conformation change
Fluorescence
Protein aggregation
Spectroscopy
 
Description 111-125
Plants under stress need to favour certain pathways so as to survive the stress period. Protection of specific enzymes by proline and other osmolytes could be one such mechanism to favour some pathways/processes. Therefore, the influence of osmolyte proline on conformational changes of various proteins caused by hydrogen peroxide (H2O2) was studied by intrinsic and extrinsic fluorescence emissions. H2O2 caused conformational change in proteins. Results indicated that for Alcohol dehydrogenase (AD) and Glutamate dehydrogenase (GD) enzymes, H2O2 induced conformational change was high and that for Glucose 6-phosphate dehydrogenase (G6PDH) and Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was low. Fluorescence and far-UV, CD measurements of catalase demonstrated that the H2O2 stabilized the protein secondary structure at low concentrations but destabilized it at higher concentrations. Intrinsic and ANS fluorescence results showed that proline at a concentration of 1.0 M prompted a reduction in the H2O2-induced exposed hydrophobic surfaces of studied enzymes, to different degrees which suggests its differential protective effect. Furthermore, SDS-PAGE studies revealed that proline was not able to reduce or inhibit the H2O2 mediated aggregation of GAPDH.
 
Date 2022-02-04T10:31:36Z
2022-02-04T10:31:36Z
2022-01
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscair.res.in/handle/123456789/59067
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJBB Vol.59(1) [January 2022]