A novel superoxide dismutase from Cicer arietinum L. Seedlings: Isolation,purification and characterization

Superoxide dismutase is an important enzyme with various therapeutic applications. search of a new source of superoxide dismutase with novel properties has significant importance. the current work reports purification of a novel superoxide dismutase enzyme with unique characteristics. a copper zinc superoxide dismutase (cu-zn sod) was purified and characterized from cicer arietinum l. seedlings germinated under aluminium (al+3) stress. the specific activity of purified protein was 158 units/mg with 28 fold purification. the superoxide dismutase is a homodimeric protein with approx subunit molecular weight of 33.27 kda. the enzyme is identified as cu-zn category of superoxide dismutase,reflected by h2o2 induced inhibition of in-gel activity and presence of quantifiable copper and zinc ions. the optimum ph range for purified cu-zn sod activity was observed within 6.5-8.5 (highest at ph 8.0) and the ph stability was in the range of 6.0-8.5. the enzyme was more stable at low temperature (below 30°c) and the km of purified cu-zn sod for riboflavin as substrate was 10.16 ± 2.5 μm. the n-terminal amino acid sequence showed homology at conserved residues with other plant cu-zn sods. © 2013 bentham science publishers.