A Novel Superoxide Dismutase from Cicer arietinum L. Seedlings: Isolation, Purification and Characterization

Author(s): Sushant Singh, Abhay Narayan Singh, Anil Verma, Vikash Kumar Dubey.

Journal Name: Protein & Peptide Letters

Volume 20 , Issue 7 , 2013

Submit Manuscript
Submit Proposal

Abstract:

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

Keywords: Protein purification, enzyme kinetics, superoxide dismutase.

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 20
ISSUE: 7
Year: 2013
Page: [741 - 748]
Pages: 8
DOI: 10.2174/0929866511320070002
Price: $58

Article Metrics

PDF: 8