Partial purification and characterization of an iodide peroxidase from Enteromorpha linza
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PURIFICATION AND SOME PARTIAL CHARACTERIZATION OF PEROXIDASE ISOENZYME FROM BRASSICA OLERACEA CAPITATA L.
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-P...
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متن کاملpurification and some partial characterization of peroxidase isoenzyme from brassica oleracea capitata l.
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-p...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1970
ISSN: 0306-3283
DOI: 10.1042/bj1190021p