Regulation of horse-liver glutathione reductase |
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| Affiliation: | 2. Departamento de Bioquimica Vegetal y Biologia Molecular, Universidad de Sevilla, 41012 Sevilla, Spain;1. The Institute for Social Development and Policy Research, Seoul National University: 220-540, 1, Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea;2. Department of Sociology, Seoul National University: 16-204, 1, Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea;3. Department of Public Health Science, Graduate School of Public Health, Seoul National University: 1, Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea;4. Institute of Health and Environment, Seoul National University: 1, Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea;1. Department of Chemistry, Acharya Narender Dev College, University of Delhi, Delhi-19, India;2. Department of Chemistry, Kirori Mal College, University of Delhi, Delhi-7, India;3. Department of Chemistry, University of Delhi, Delhi-7, India;1. Polymer Institute, Slovak Academy of Sciences, Dubravska cesta 9, 845 41 Bratislava, Slovakia;2. Faculty of Chemical and Food Technology, Slovak University of Technology in Bratislava, Radlinskeho 9, 812 37 Bratislava, Slovakia |
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| Abstract: | - 1.1. The enzyme was rapidly inactivated by NAD(P)H, GSH, dithionite or borohydride, while activity increased in the presence of NAD(P)+ or GSSG. NADH was more efficient for inactivation than NADPH. Redox inactivation required neutral or alkaline pH, was maximal at pH 8.5, and depended on the presence of metal cations.
- 2.2. GSSG and dithiothreitol fully protected the enzyme from inactivation at concentrations stoichiometric with NAD(P)H. Ten-fold higher ferricyanide or GSH concentrations were required to obtain partial protection. NAD+ or NADP+ were quite ineffective.
- 3.3. GSSG fully reactivated the inactive enzyme at 38°C and neutral to acidic pH (5.5–7.5). Reactivation by dithiothreitol was accomplished in short periods of time at pH 8.5 although the activity was progressively lost afterwards. Ferricyanide and GSH also reactivated the enzyme to different extents.
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