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Two-dimensional Electrophoretic Analysis of Nucleotide phosphate Kinase Mediated Hydrogen Peroxide Cross-linking in Saccharamyces cerevisiae  

Moon Hae-Jeong (Industrial Liaison Research Institute)
Yun Dae-Jin (Department of Chemical Engineering, Kyung Hee University)
Park Chang-Ho (Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University)
Publication Information
KSBB Journal / v.21, no.1, 2006 , pp. 16-19 More about this Journal
Abstract
Oxidative modification of nucleoside diphosphate kinase (NDPK) is identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometer. The quaternary structure of NDPK appears to be regulated by cross-linking with an oxidant, $H_2O_2$. We compared roles of NDPK in each of wild type and ynk mutant against oxidative stress. Six specific proteins changed by $H_2O_2$ were identified using two-dimensional electrophoretic analysis. YNK regulated several proteins, related to $H_2O_2$ signaling functions. These results suggest that one of the important functions of NDPK is the regulation of cellular redox state.
Keywords
NDPK; two-dimensional electrophoretic analysis; ynk mutant; MALDI-TOF MS;
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