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POLYCLONAL ANTIBODIES AGAINST IRON‐SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI B CROSS‐REACT WITH SUPEROXIDE DISMUTASES FROM SYMBIODINIUM MICROADRIATICUM (DINOPHYCEAE) 1
Author(s) -
Matta Jaime L.,
Govind Nadathur S.,
Trench Robert K.
Publication year - 1992
Publication title -
journal of phycology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.85
H-Index - 127
eISSN - 1529-8817
pISSN - 0022-3646
DOI - 10.1111/j.0022-3646.1992.00343.x
Subject(s) - polyclonal antibodies , superoxide dismutase , biology , escherichia coli , biochemistry , molecular mass , microbiology and biotechnology , dinoflagellate , dismutase , antibody , enzyme , gene , botany , immunology
Assays for superoxide dismutases (SODs) were performed using cell‐free extracts of the symbiotic dinoflagellate Symbiodinium microadriaticum Freudenthal (emend Trench and Blank) after separation in undenatured polyacrylamide gels. Using appropriate inhibitors (KCN and H 2 O 2 ) we detected the presence of Cu/Zn‐, Mn‐, and Fe‐SODs. In immunoblot assays, polyclonal antibodies against Fe‐SOD from Escherichia coli B cross‐reacted with two major polypeptides in the water‐soluble fraction and one polypeptide in the Triton X‐100‐solubilized pellet fraction. The polypeptide common to both fractions, with a relative molecular mass of 43.5 kDa, was identified as Mn‐SOD. In S. microadriaticum , FeSOD, found only in the water‐soluble fraction, appears to be monomeric, with a relative molecular mass of 49.5 kDa.