purification and characterization of highly stable aldo-keto reductase from camel (camelus dromedarius) liver

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ID: 206463
2013
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Abstract
Aldo-keto reductase (AKR) was purified to homogeneity from camel liver by ion exchange on Q Sepharose, affinity chromatography on Blue-Sepharose and 2,5-ADP-Sepharose 4B. The purification procedure resulted in 32.43-fold purification with 0.65% final yield. Subunit and native molecular weights of the purified enzyme determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography, were 33kD and 133kD, respectively. The purified AKR exhibited maximal activity at a temperature of 50°C and pH of 7.0. The Km values for NADPH and NADH calculated from the Lineweaver-Burk plot were 0.01 mM and 0.083 mM, respectively, whereas the Km values for m-Nitrobenzaldehyde, 4-Anisaldehyde and P-Benzoquinone were 0.9 mM, 1.11 mM and 0.57 mM, respectively.
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Authors Al-Harbi Ibrahim A., Al-Senaidy Abdurrahman M., Ismael Mohammad A.
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Journal gastrointestinal endoscopy
Year 2013
DOI
10.2298/ABS1301113A
URL
http://www.doiserbia.nb.rs/img/doi/0354-4664/2013/0354-46641301113A.pdf
Keywords
Characterization purification aldo-keto reductase camel

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