|
KMID : 0377519870120010065
|
|
Chung-Ang Journal of Medicine
1987 Volume.12 No. 1 p.65 ~ p.74
|
|
|
Studies on Partial Purification and Characterization of Peroxidase from Human Term Placenta
|
|
|
|
|
Abstract
|
|
|
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 Putter(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 sulfate precipitation and DEAE-cellulose column chromatography.
3. The most rapidly oxidized substrate was o-dianisidine. Benzidine, ascorbic acid and guaiacol were oxidized with decreasing order of rates, while oxidation of dihydroxyphenols and trihydroxyphenol were very slow.
4. The partially purified peroxidase was strongly inhibited by 1. 0 mM of sulfhydryl reagents and cyanide.
5. The optimal temperature for enzyme activity was 40C and the optimal pH was 5.5.
6. The half life of the enzyme activity was 30 min. at 60C.
T The Km values for hydrogen peroxide and guaiacol of peroxidase were 0.50 mN1 and 0.44 mil, respectively.
8. The purified enzyme was a typical hemoprotein.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|