Copper-zinc superoxide dismutase from Ascaris suum (Nematoda): purification and characterization.
Copper-zinc superoxide dismutase from Ascaris suum (Nematoda) was purified in a new, more efficient, and faster manner. The process included differential centrifugation, fractionation with ammonium sulfate, and sodium dodecyl sulfate-polyacrylamide electrophoresis, yielding a 340-fold purification (specific activity of 47 units/mg). Optimal storage conditions, optimal pH range, thermostability, molecular weight and ultraviolet-visible absorption spectrum of the enzyme are described, and a new enzymatic model for pharmacological screening is suggested.
Sanchez-Moreno
M
M
Department of Biochemistry and Molecular Biology Faculty of Sciences, University of Granada, Spain.
Entrala
E
E
Janssen
D
D
Osuna
A
A
D000645:Ammonium Sulfate; D000818:Animals; D017165:Ascaris suum / Q000201:enzymology*; D002498:Centrifugation; D005591:Chemical Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013053:Spectrophotometry; D013482:Superoxide Dismutase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
D013482:Superoxide Dismutase; D000645:Ammonium Sulfate