1. 1. Two glutathione peroxidases (GSH-Px), D1 and D2, were partially purified from the hepatopancreas of common carp Cyprinus carpio by ion-exchange, gel filtration, and hydrophobic chromatography. The enzymatic properties of those enzymes were examined. 2. 2. The D1 and D2 differed in following enzymatic properties. The pH optima of D1 and D2 were 8.0 and 9.0, respectively. 3. 3. When stored at pH 4.0 for 36 hr, D1 kept 70% of maximal activity while only 30% of that was shown in D2. 4. 4. D1 and D2 lost activity by 50% when incubated at 55°C and 65°C for 10 min, respectively.
|Number of pages||5|
|Journal||Comparative Biochemistry and Physiology -- Part B: Biochemistry and|
|Publication status||Published - 1992 May|
ASJC Scopus subject areas
- Molecular Biology