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<em>In vitro</em> stability of various enzymes by proline from H2O2 mediated oxidative damage

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Title Statement <em>In vitro</em> stability of various enzymes by proline from H2O2 mediated oxidative damage
 
Added Entry - Uncontrolled Name Kumar Dalal, Vijay
K Biswal, Ajay
Patel, Dhawal
Subramanyam, Rajagopal
S Raghavendra, Agepati
 
Uncontrolled Index Term ANS; CD; Conformation change; Fluorescence; Protein aggregation; Spectroscopy
 
Summary, etc. 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.
 
Publication, Distribution, Etc. Indian Journal of Biochemistry and Biophysics (IJBB)
2022-02-03 00:00:00
 
Electronic Location and Access application/pdf
http://op.niscair.res.in/index.php/IJBB/article/view/45560
 
Data Source Entry Indian Journal of Biochemistry and Biophysics (IJBB); IJBB Vol. 59 (1) [January 2022]
 
Language Note en