Purification and Kinetics of Bovine Kidney Cortex Glutathione Reductase

Tandogan, Berivan; Ulusu, Nuriye Nuray

doi:10.2174/092986610791112684

Cited by 14 publications

(12 citation statements)

References 25 publications

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“…In contrast, in sheep brain cortex, it followed a Theorell–Chance mechanism. The distinct kinetic mechanisms highlight the various enzyme modifications that have taken place, including post-translational modifications at the molecular level (Ulusu et al 1999, 2005; Ulusu and Tandogan 2006, 2007; Tandogan and Ulusu 2010; Ulusu and Sengezer 2012). …”

Section: Complexity Of Kinetic Mechanismsmentioning

confidence: 99%

Evolution of Enzyme Kinetic Mechanisms

Ulusu

2015

J Mol Evol

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This review paper discusses the reciprocal kinetic behaviours of enzymes and the evolution of structure–function dichotomy. Kinetic mechanisms have evolved in response to alterations in ecological and metabolic conditions. The kinetic mechanisms of single-substrate mono-substrate enzyme reactions are easier to understand and much simpler than those of bi–bi substrate enzyme reactions. The increasing complexities of kinetic mechanisms, as well as the increasing number of enzyme subunits, can be used to shed light on the evolution of kinetic mechanisms. Enzymes with heterogeneous kinetic mechanisms attempt to achieve specific products to subsist. In many organisms, kinetic mechanisms have evolved to aid survival in response to changing environmental factors. Enzyme promiscuity is defined as adaptation to changing environmental conditions, such as the introduction of a toxin or a new carbon source. Enzyme promiscuity is defined as adaptation to changing environmental conditions, such as the introduction of a toxin or a new carbon source. Enzymes with broad substrate specificity and promiscuous properties are believed to be more evolved than single-substrate enzymes. This group of enzymes can adapt to changing environmental substrate conditions and adjust catalysing mechanisms according to the substrate’s properties, and their kinetic mechanisms have evolved in response to substrate variability.

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Section: Complexity Of Kinetic Mechanismsmentioning

confidence: 99%

Evolution of Enzyme Kinetic Mechanisms

Ulusu

2015

J Mol Evol

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“…We have purified GR from bovine liver and kidney cortex and then analyzed the effect of RA on the purified enzyme (Ulusu & Tandogan, 2007;Tandogan & Ulusu, 2010). Baker's yeast GR is obtained from Sigma and the specific activity of the enzyme is 1.25 U/mg.…”

Section: Resultsmentioning

confidence: 99%

“…Bovine kidney cortex and liver GR is purified by chromatography consisting of two steps after ultracentrifugation by Beckman L7-80 ultracentrifuge and heat denaturation: 2′,5′-ADP Sepharose 4B affinity and DEAE Sepharose Fast Flow anion exchange chromatography (Ulusu & Tandogan, 2007;Tandogan & Ulusu, 2010). Bovine liver GR was purified 28,028-fold with a final yield of 43%.…”

Section: Purification Of Grmentioning

confidence: 99%

In vitroeffects of rosmarinic acid on glutathione reductase and glucose 6-phosphate dehydrogenase

Tandogan

Kuruüzüm-Uz

Sengezer

et al. 2011

Pharmaceutical Biology

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“…Potential sites of action of long‐acting somatostatin analogues on aldose reductase and GLUT 3 are shown in green. Key enzymes and their kinetic parameters are as follows: (A) Glutathione reductase (E.C.1.6.4.2) Km NADPH 8–21 μM, Km GSSG 26–65 μM; Carlberg & Mankervik ; Tandogan & Ulusu . (B) Aldose reductase (E.C.…”

Section: Discussionmentioning

confidence: 99%

Effects of long‐acting somatostatin analogues on redox systems in rat lens in experimental diabetes

Kunjara

Greenbaum

Sochor

et al. 2014

Int J Experimental Path

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The effects of long-acting somatostatin analogues, angiopeptin (AGP) and Sandostatin (SMS), on the early decline in the lens content of glutathione (GSH), ATP and NADPH and increase in sorbitol were studied in STZ diabetic rats, and comparison was made with the effect of insulin. Three factors prompted this study: (i) the known increase in IGF-1 in ocular tissue in diabetes and antagonistic effect of somatostatins, (ii) the known effect of IGF-1 in increasing lens aldose reductase and (iii) the lack of effect of somatostatins on diabetic hyperglycaemia, the latter enabling a differentiation to be made between effects of hyperglycaemia per se and site(s) of IGF-1/somatostatins. All four metabolites studied showed a significant restoration towards the normal control level after 7 days of treatment with AGP and SMS, and AGP was more effective on levels of GSH and ATP. A significant correlation was found between GSH and ATP across all groups at 7 days treatment. The redox state changes in diabetes include both NADP+/NADPH and NAD+/NADH in the conversion of glucose to sorbitol and via sorbitol dehydrogenase to fructose with a linked decrease in ATP formation via NAD+/NADH regulation of the glycolytic pathway. The interlinked network of change includes the requirement for ATP in the synthesis of GSH. The present study points to possible loci of action of somatostatins in improving metabolic parameters in the diabetic rat lens via effects on aldose reductase and/or glucose transport at GLUT 3.

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Purification and Kinetics of Bovine Kidney Cortex Glutathione Reductase

Cited by 14 publications

References 25 publications

Evolution of Enzyme Kinetic Mechanisms

Evolution of Enzyme Kinetic Mechanisms

In vitroeffects of rosmarinic acid on glutathione reductase and glucose 6-phosphate dehydrogenase

Effects of long‐acting somatostatin analogues on redox systems in rat lens in experimental diabetes

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