Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex

Ulusu, Nuriye Nuray; Tandogan, Berivan; Tezcan, Ferhan E.

doi:10.1016/j.biochi.2004.11.002

Cited by 27 publications

(25 citation statements)

References 19 publications

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“…According to these results, GR is the most resistant enzyme against temperature. This result is also in parallel with similar results in the literature 16,35,[45][46][47][48] . For calculation of stable pH of enzymes, 200 mM phosphate buffers with 5.5, 6.0, 6.5, 7.0 and 7.5 pH, and 200 mM Tris-HCl buffers with 8.0, 8.5 and 9.0 pH were preserved at +4 C together with the equal amount of enzyme solution, and activity measurements were performed for 72 h with 12 h intervals.…”

Section: Discussionsupporting

confidence: 82%

“…We observed that NADPH efficiently inhibited the G6PD enzyme and inhibition type was determined as uncompetitive. The inhibition type of NADPH on G6PD enzyme from different origin was reported as noncompetitive and competitive, but, the inhibition type on rat lung G6PD is unlike to that in the previous studies 13,16,50,51 . 6PG has the lower affinity towards 6PGD when compared with NADP + since the K M for 6PGA is higher than that for NADP + .…”

Section: Discussioncontrasting

confidence: 51%

“…They have been purified from several mammalian tissues with various techniques such as rat liver and kidney [8][9][10] , human erythrocyte 11,12 , rat small intestine 13 , grass carp hepatopancreases 14 , rainbow trout liver 15 and lamb kidney 16 , and some of their characteristics and kinetic properties have been determined.…”

Section: Introductionmentioning

confidence: 99%

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Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Adem

Çiftçi

2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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G6PD, 6PGD and GR have been purified separately in the single step from rat lung using 2 0 , 5 0 -ADP Sepharose 4B affinity chromatography. The purified enzymes showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weights of the enzymes were estimated to be 134 kDa for G6PD, 107 kDa for 6PGD and 121 kDa for GR by Sephadex G-150 gel filtration chromatography, and the subunit molecular weights was respectively found to be 66, 52 and 63 kDa by SDS-PAGE. Optimum pH, stable pH, optimum ionic strength, optimum temperature, K M and V max values for substrates were determined. Product inhibition studies were also performed. The enzymes were inhibited by levofloxacin, furosemide, ceftazidime, cefuroxime and gentamicin as in vitro with IC 50 values in the range of 0.07-30.13 mM. In vivo studies demonstrated that lung GR was inhibited by furosemide and lung 6PGD was inhibited by levofloxacin.

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Section: Discussionsupporting

confidence: 82%

Section: Discussioncontrasting

confidence: 51%

See 1 more Smart Citation

Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Adem

Çiftçi

2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Dog liver G6PD had an optimum pH of 7.8 [3]. Lamb kidney cortex G6PD had an optimum pH between 7.6 and 7.8 [40]. Sheep kidney cortex G6PD had an optimum pH of 7.4 [5].…”

Section: Discussionmentioning

confidence: 98%

Biochemical Characterization of Buffalo Liver Glucose-6-Phosphate Dehydrogenase Isoforms

et al. 2015

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Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme involved in the pentose phosphate pathway. This works represents purification of two buffalo liver glucose-6-phosphate dehydrogenases (BLG6PD1 and BLG6PD2) using combination of ammonium sulfate precipitation and several chromatographic columns. Both enzymes (BLG6PD1 and BLG6PD2) were homogenous on both native PAGE as well as 12% SDS PAGE with molecular weights of 28 and 66 kDa. The molecular weight of BLG6PD1 and BLG6PD2 native forms were determined to be 28 and 66 kDa by gel filtration; indicating monomeric proteins. The K(m) values for BLG6PD1 and BLG6PD2 estimated to be 0.059 and 0.06 mM of β-nicotinamide adenine dinucleotide phosphate. The optimum activity of BLG6PD1 and BLG6PD2 were displayed at pH 8.0 and 8.2 with an isoelectric point (pI) of pH 7.7-7.9 and 5.7-5.9. The divalent cations MgCl2, and CoCl2 act as activators, on the other hand, FeCl2, CuCl2 and ZnCl2 are potent inhibitors of BLG6PD1 and BLG6PD2 activity. NADPH inhibited both isoenzymes competitively with Ki values of 0.012 and 0.030 mM. This study describes a reproducible purification scheme of G6PD from the liver of buffalo as a rich source.

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“…G6PD catalyzes the transformation of G6P to 6-phosphogluconolactone and reduction of co-enzyme nicotinamide adenine dinucleotide phosphate to NADPH by different kinetic mechanisms in different organisms. It has been shown that G6PD catalyzes the reaction by ordered Bi Bi mechanism in Schizosaccharomyces pombe [24] mouse liver [25] lamb kidney cortex [26] Corynebacterium glutamicum [27] Acetobacter hansenii (formerly known as Acetobacter xylinum) [28] bovine lens [6]. Random Bi Bi mechanism is investigated in Plasmodium falciparum [29], Taenia crassiceps (Eucestoda: Cyclophyllidea) [30], Aspergillus aculeatus, a filamentous fungus [31], Aspergillus niger and Aspergillus nidulans [32].…”

Section: Kinetic Mechanism Productmentioning

confidence: 99%

Kinetic mechanism and some properties of glucose-6-phosphate dehydrogenase from sheep brain cortex

Ulusu

Sengezer

2012

Turk J Bioch

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Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex

Cited by 27 publications

References 19 publications

Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Biochemical Characterization of Buffalo Liver Glucose-6-Phosphate Dehydrogenase Isoforms

Kinetic mechanism and some properties of glucose-6-phosphate dehydrogenase from sheep brain cortex

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