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| Article Name : | | | BIOCHEMICAL CHARACTERIZATION OF PEROXIDASE FROM CALOTROPIS PROCERA LATEX | | Author Name : | | | Omar A.M. Al-Bar | | Publisher : | | | Ashok Yakkaldevi | | Article Series No. : | | | ROR-1183 | | Article : | |  | Author Profile | | Abstract : | | | Peroxidase from Calotropisproceralatex was purified by benzene treatment, DEAE-Sepharose and Sephacryl S-200 column. The purity was determined from the high specific activity (2200 units/mg protein), purification fold (7.0), and a single band in native PAGE, SDS-PAGE. Peroxidase had molecular mass of 45 kDa. Phenylenediamine had the highest peroxidase activity (140%), o-dianisidine had moderate activity (83%). p-Aminoantipyrine (42%) and pyrogallol (33%) had low affinity towards enzyme. The apparent Km value ofperoxidase from C. procera latex for H2O2 and guaiacol were 6.8 and 11.4 mM/ml, respectively. The enzyme showed a pH optimum at 5.5, whereasthe optimal temperature was 40°C. The enzyme activity was remained stable up to 40˚C. Both Cu2+ and Fe2+ caused the highest activation at 2 and 5 mM (260, 115 and 290, 230%, respectively). Hg2+ caused the highest inhibitory effect. In conclusion, Calotropisproceralatex could be a new and potential source for peroxidase enzyme. | | Keywords : | | - Characterization
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