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      • 마늘중 Peroxidas 의 정제 및 이의 특성에 관한 연구

        조성희,차인돈 中央大學校 自然科學硏究所 1988 自然科學硏究所 論文集 Vol.2 No.-

        Peroxidase was purified from garlic and observed its some biochemical properties. The experimental results were summarized as follows. 1. The peroxidase from garlic was purified about 32.4 fold by ammonium sulfate precipitation and DEAE-cellulose column chromagagraphy. 2. The more rapidly oxidized suvstrate was o-dianisidine, while benzine, guaiacol, and pyrogllol were oxidized with dereasing rates. But the oxidation of dihydroxyphenols and L-ascorbic acid were negligble. 3. The DTT and 2-mercaptoethanol have inhibited 100% of peroxidase activity at conentrations of 10mM and 1mM. but the peroxidase was slightly inhibited by EDTA and urea at the same concentrations. 4. The optimum temperature was 55℃ 5. The optimum pH was 5.6. 6. The Km values for hydrogen peroxide and guaiacol of purified peroxidase were 2mM and 0.9mM, respectively.

      • 사람 태반조직 Peroxidase의 부분정제 및 특성에 관한 연구

        황윤영,차인돈,이희성 중앙대학교 의과대학 의과학연구소 1987 中央醫大誌 Vol.12 No.1

        The purification and some properties of peroxidase of human term placenta was made in this study. The activity of peroxidase was measured by the method of Pu‥tter(1974). The results were summarized as follows; 1. The activity of peroxidase in cytosolic fraction of human term placenta was found to be 31.09 units per g wet tissue. 2. The peroxidase from human term placenta was purified about 22-fold by ammonium sulface precopitation and DEAE-cellulose column chromatography. 3. The most rapidly oxidized substrate was o-dianisidine. Benzidine, ascordic acid and guaiacol were oxidized with decreasing order of rats, while oxidation of dihydrooxyphenols and trihydrooxyphenol were very slow. 4. The partially purified peroxidase was strongly inhibited by i.omM of sulfhydryl reagents and cyanide. 5. The optimal tempreature for enzyme astivity was 40℃ and the optimal pH was 5.5. 6. The half life of the enzyme astivity was 30 min. at 60℃. 7. the Km values for hydrogen peroxid and guaiacol of peroxidase were 0.50mM and 0.44mM, respectively. 8. The purified enzyme was a typical hemoprotein.

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