ArticleEnzyme research2014
Purification and characterization of glucose-6-phosphate dehydrogenase from camel liver.
Article in Enzyme research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Biochemical and Kinetic Characterization of the Glucose-6-Phosphate Dehydrogenase fromMicroorganisms · 2022Article
- Identification and In Silico Characterization of NovelMolecules (Basel, Switzerland) · 2021Article
- The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH.Metabolites · 2020Review
- Characterizing the Fused TvG6PD::6PGL Protein from the ProtozoanInternational journal of molecular sciences · 2020Article
- Molecular Cloning and Exploration of the Biochemical and Functional Analysis of Recombinant Glucose-6-Phosphate Dehydrogenase fromInternational journal of molecular sciences · 2019Article
- Cloning, Expression, and Characterization of a Psychrophilic Glucose 6-Phosphate Dehydrogenase fromInternational journal of molecular sciences · 2019Article
- Biochemical Characterization and Structural Modeling of Fused Glucose-6-Phosphate Dehydrogenase-Phosphogluconolactonase fromInternational journal of molecular sciences · 2018Article
- Biochemical characterization of buffalo liver glucose-6-phosphate dehydrogenase isoforms.The protein journal · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glucose-6-phosphate dehydrogenase from camel liver was purified to homogeneity by ammonium sulfate precipitation and a combination of DEAE-cellulose, Sephacryl S-300 gel filtration, and 2', 5' ADP Sepharose 4B affinity chromatography columns. The specific activity of camel liver G6PD is increased to 1.80438 units/mg proteins with 63-fold purification. It turned out to be homogenous on both native PAGE and 12% SDS PAGE, with a molecular weight of 64 kDa. The molecular weight of the native form of camel liver G6PD was determined to be 194 kDa by gel filtration indicating a trimeric protein. The K m value was found to be 0.081 mM of NADP(+). Camel liver G6PD displayed its optimum activity at pH 7.8 with an isoelectric point (pI) of pH 6.6-6.8. The divalent cations MgCl2, MnCl2, and CoCl2 act as activators; on the other hand, CaCl2 and NiCl2 act as moderate inhibitors, while FeCl2, CuCl2, and ZnCl2 are potent inhibitors of camel liver G6PD activity. NADPH inhibited camel liver G6PD competitively with K i value of 0.035 mM. One binding site was deduced for NADPH on the enzyme molecule. This study presents a simple and reproducible purification procedure of G6PD from the camel liver.
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Registered trials
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