تعداد نشریات | 158 |
تعداد شمارهها | 6,230 |
تعداد مقالات | 67,765 |
تعداد مشاهده مقاله | 115,201,016 |
تعداد دریافت فایل اصل مقاله | 89,948,920 |
PURIFICATION AND SOME PARTIAL CHARACTERIZATION OF PEROXIDASE ISOENZYME FROM BRASSICA OLERACEA CAPITATA L. | ||
Journal of Sciences, Islamic Republic of Iran | ||
مقاله 2، دوره 13، شماره 2، شهریور 2002 اصل مقاله (263.98 K) | ||
چکیده | ||
Acetone fractionated peroxidase from crude extract of Brassica oleracea leaves (Cabbage) was purified in three steps on chromatographic columns, using Sp-Sepharose, DEAE-Sepharose and Con A-Sepharose. The specific activity of purified main isoenzyme (BOC-POD) is 1887 u/mg protein with RZ: 3.1, which is 172 times more than the RZ of crude extract with 4.3% recovery. The molecular weight of BOC-POD is about 45,000 Dalton. Maximum pH, thermal activity and stability of this purified enzyme are also determined. Km of this isoenzyme was measured by Linewearver-Burk curve for O-dianisidine towards H2O2. This purified enzyme could be used in manufacturing diagnostic kits. | ||
عنوان مقاله [English] | ||
- | ||
چکیده [English] | ||
- | ||
آمار تعداد مشاهده مقاله: 1,038 تعداد دریافت فایل اصل مقاله: 1,876 |