|
KMID : 0377519860110030185
|
|
Chung-Ang Journal of Medicine
1986 Volume.11 No. 3 p.185 ~ p.193
|
|
|
Studies on Characterization and Partial Purification of Peroxidase
|
|
|
|
|
Abstract
|
|
|
a peroxidase has been purified to about 33 fold from sweet potatos using ammonium sulfate precipitation and DE1E-cellulose batch technique. Some biochemical properties of this partially purified enzyme were observed. The most rapidly oxidized substrate was o-d;anisid;ne. Benzidine, pyrogalloi and gaaiacol were oxidized with decreasing order of rates, while oxidation of dihydroxy-phenols was very slow. This
.,
enzyme´ was remarkably inhibited by 1. OmM of sulfhydryl reagents and cyanide but EDT. and iodoacetamide did not. The thermal inactivation of peroxidase occured above 60C. After heat treatment at 7.9´ C for 10mir., the reactivation of enzyme by cooling to 4C -was observed at pH 7. 0. Therefore the mecha nism of heat´ inactivation seems to be due to the splitting of prosthetic group from holoenzyme. The purified´ enzyme was a typical heme and glycoprotein, and activation energy was. 5. 47KCal/mol.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|