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Purification and immunological characterization of superoxide dismutase of the onion maggot, Delia antiqua
Author(s) -
Ishikawa Yukio
Publication year - 1995
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940280408
Subject(s) - superoxide dismutase , isoelectric focusing , biology , isoelectric point , biochemistry , molecular mass , size exclusion chromatography , protein subunit , polyacrylamide gel electrophoresis , ammonium sulfate precipitation , dismutase , enzyme , microbiology and biotechnology , gene
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‐PAGE revealed only one subunit of 16,000 daltons, indicating that SOD is a homodimer. Isoelectric 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 (aSOD1H11) recognized SOD of Drosophila melanogaster as well. © 1995 Wiley‐Liss, Inc.