Partial purification and properties of glutathione peroxidase from carp hepatopancreas

T. Nakano, M. Sato, M. Takeuchi

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)31-35
    Number of pages5
    JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
    Volume102
    Issue number1
    DOIs
    Publication statusPublished - 1992 May

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Molecular Biology

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