%0 Journal Article
%T Extraction, Partial Purification and Characterization of 5¡¯-Phosphodiesterase from Germinated Phaseolus mungo (Mung Bean)
%A Nilesh Mahadeo Khutle
%A Dr.C.Vijaya
%A Harshal Pawar
%A Priti Jodhe
%J International Journal of Pharmaceutical and Phytopharmacological Research
%D 2011
%I International Journal of Pharmaceutical and Phytopharmacological Research
%X 5¡¯-Phosphodiesterase (5¡¯-PDE) is an enzyme that hydrolyses RNA to a mixture of ribonucleotide, from which 5¡¯-guanosine monophosphate (5¡¯-GMP) and 5¡¯-Inosine monophosphate (5¡¯-IMP) can be isolated. In the present work 5¡¯PDE was extracted and partially purified from germinated mung bean. 5¡¯-PDE activity was monitored using bis-(p-nitro phenyl phosphate) disodium salt as the substrate. The enzyme acts on substrate and releases the p-nitrophenol, which is measured at 420 nm. Purification was carried out by centrifugation, Ammonium sulphate precipitation followed by membrane filtration and heat shock treatment which gave 6.41-fold concentration. The enzyme had a pH optimum of 6.0 and showed good stability over pH range from 4 to 7.The optimum temperature for enzyme activity was found to be 600C and was also found stable at 40C.5¡¯-PDE activity was enhanced up to 147% in the presence of Mg++. MichelisMenten equation with km 0.48 and Vmax 19230 was determined from Lineweaver Burke plot. This partially purified enzyme could be used for hydrolysis of RNA to produce 5¡¯-GMP and 5¡¯-adenosine monophosphate, a precursor of 5¡¯-IMP.
%K 5¡¯-Phospodiesterase
%K Germinated mung bean
%K Purification
%K 5¡¯-GMP
%K 5¡¯-IMP
%U http://www.eijppr.com/3.Extraction,%20Partial%20Purification%20and%20Characterization%20of%205%92-Phosphodiesterase%20from%20Germinated%20Phaseolus%20mungo%20(Mung%20Bean)%20(1).pdf