Abstract
Two electrophoretically distinguishable variants of Superoxide dismutase (SOD) are common in natural populations of Drosophila melanogaster. We have earlier comparatively characterized these two electromorphs, SOD F and SOD S By peptide mapping in high-performance liquid chromatography (HPLC), we now show that the difference between the two electromorphs is due to the replacement of Asn-96 (SOD F) by Lys-96 (SOD s). It is far from clear how this replacement causes the biochemical differences (in thermostability, specific activity, and others) observed between these two forms of the enzyme.
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