Isolation, purification and characterization of Plasmodium yoelii adenosine deaminase for clinical use
Plasmodium yoelii like many other parasitic protozoans is deficient of having the advantage of the de novo pathway for purine biosynthesis and starkly acts upon the salvage pathway. Adenosine deaminase (Also known as adenosine aminohydrolase or ADA; EC 126.96.36.199), the first enzyme of the pathway was purified from Plasmodium yoelii, a rodent malarial species by using ammonium sulphate precipitation cut column chromatography by DEAE-Sephadex ion exchange column and Sephadex G-100 gel filtration column in successive steps and the activity of ADA was estimated afterwards. The purity of ADA was checked on 10% SDS–PAGE followed by the conduction of Western Blot to analyze the molecular weight of obtained ADA. After carrying out the western blot technique, the electrophoresis data interpreted that the purified enzyme is monomeric having the molecular weight of 41 KD. The specific activity of ADA was increased in each purification step indicating that protein was purified in each step. The enzyme was found to be pure to ~10 folds. By thwarting the requirement as well as the effect of ADA, potential anti-malarial drugs can be designed against the rage of Plasmodium yoelii and other parasitic protozoans and this may serve the purpose to a great extent.
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