Affinity chromatography of succinate dehydrogenase from the membranes of Micrococcus lysodeikticus.
Isolated plasma membranes of Micrococcus lysodeikticus were subjected to extraction with n-butanol in a two-phase system. Succinate dehydrogenase obtained in the soluble aqueous phase after high-speed centrifugation was resolved by separation on calcium phosphate gel and affinity chromatography. The affinity ligand used was oxaloacetate and elution from the column was achieved with 0.5 M succinate. In the final product there was an eleven-fold reduction in the 32P-lipid to protein ratio and a fourteen-fold increase in specific activity relative to the high speed supernatant fraction following n-butanol extraction.
D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity / Q000379:methods; D008837:Micrococcus / Q000201:enzymology*; D010071:Oxaloacetates; D010743:Phospholipids / Q000032:analysis; D011485:Protein Binding; D013385:Succinate Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism
D010071:Oxaloacetates; D010743:Phospholipids; D013385:Succinate Dehydrogenase