Purification and immunological characterization of superoxide dismutase of the onion maggot, Delia antiqua

✍ Scribed by Dr. Yukio Ishikawa

• Publisher: John Wiley and Sons
• Year: 1995
• Tongue: English
• Weight: 566 KB
• Volume: 28
• Category: Article
• ISSN: 0739-4462
• DOI: 10.1002/arch.940280408

✦ Synopsis

Cytosolic superoxide dismutase (SOD) of the onion maggot, Delia antiqua, was purified to apparent homogeneity by ammonium sulfate fractionation followed by anion exchange, hydrophobic interaction, and gel filtration chromatographies. Native molecular mass was estimated as 32,000 daltons. SDS-PACE revealed only one subunit of 16,000 daltons, indicating that SOD is a hornodimer. lsoelectric focusing revealed 3 charge isomers of pls 5.3, 5.5, and 5.7. The specific activity of purified SOD was 4,250 U/mg protein. A monoclonal antibody (MAb, aSOD2B7) raised against Delia SOD recognized only SOD of the same genus, but another MAb (aSODlH11) recognized SOD of Drosophila melanogaster as well. o 1995 Wiiey-Liss, inc.