Purification and characterization of a Cu, Zn-superoxide dismutase from adult Paragonimus westermani.
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.
Chung
Y B
YB
Department of Biology, College of Natural Sciences, Chung-Ang University, Seoul, Korea.
Song
C Y
CY
Lee
H S
HS
Kong
Y
Y
Cho
S Y
SY
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D008970:Molecular Weight; D010238:Paragonimus / Q000201:enzymology*; D013482:Superoxide Dismutase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D013482:Superoxide Dismutase