PURIFICATION AND PARTIAL CHARACTERIZATION O F PEROXIDASES FROM CULTIVATED RAPHANUS SATIVUS L. VAR. CICIL
نویسندگان
چکیده مقاله:
Two peroxidases (EC. 1.11.1.7), POD I and POD II were purified from the roots of cultivatedRaphanus sativus L. Var. Cicil by one step ion-exchange chromatography after fractionation by acetone. The molecular weight of these enzymes were 43000 and 41000 Daltons and RZ 1.2 and 2.0 for POD I and POD II, respectively. Both enzymes consisted of a single polypeptide chain on SDS-PAGE. The maximum activity of POD I was observed at pH 4.6 and 30°C and for POD II, at pH 6.5 and 60°C. The Km value of POD I for H202 was 7.26 mM and for POD II, 2 mM toward o-dianisidin. Both isoenzymes were stable for 48 hours in temperatures up to 40°C and stable in pH 4-8 for 3 hours.
منابع مشابه
purification and partial characterization o f peroxidases from cultivated raphanus sativus l. var. cicil
two peroxidases (ec. 1.11.1.7), pod i and pod ii were purified from the roots of cultivatedraphanus sativus l. var. cicil by one step ion-exchange chromatography after fractionation by acetone. the molecular weight of these enzymes were 43000 and 41000 daltons and rz 1.2 and 2.0 for pod i and pod ii, respectively. both enzymes consisted of a single polypeptide chain on sds-page. the maximum act...
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عنوان ژورنال
دوره 12 شماره 3
صفحات 273- 277
تاریخ انتشار 1998-11
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