Korean J Parasitol.  1991 Sep;29(3):259-266. 10.3347/kjp.1991.29.3.259.

Purification and characterization of a Cu, Zn-superoxide dismutase from adult Paragonimus westermani

• Chung YB
• Song CY
• Lee HS
• Kong Y
• Cho SY

• KMID: 1715551
• DOI: http://doi.org/10.3347/kjp.1991.29.3.259

Abstract

In cytosolic fraction of adult Paragonimus westermani, superoxide dismutase activity was identified (4.3 units/mg of specific activity) using a xanthine-xanthine oxidase system. The enzyme was purified 150 fold in its activity using the ammonium sulfate precipitation, DEAE-Trisacryl M anion-exchange chromatography and Sephadex G-100 molecular sieve chromatography. The enzyme exhibited the enhanced activity at pH 10.0. The enzyme activity totally disappeared in 1.0mM cyanide while it remained 77.8% even in 10 mM azide. These findings indicated that the enzyme was Cu, Zn-SOD type. Molecular mass of the enzyme was estimated to be 34 kDa by gel filtration and 17 kDa on reducing SDS-polyacrylamide gel electrophoresis which indicated a dimer protein.

MeSH Terms

Cytosol-enzymology
Molecular-Weight
Superoxide-Dismutase-chemistry
Superoxide-Dismutase-metabolism
*Paragonimus-enzymology
*Superoxide-Dismutase-isolation-and-purification
Superoxide-Dismutase