Purification and properties of succinyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney

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Abstract
CoA-transferase (succinyl-CoA-3-oxo acid CoA-transferase, EC 2.8.3.5) isolated from sheep kidney was purified to homogeneity. The purified enzyme has a specific activity of approximately 200 units/mg. A MW of 110,000 was obtained by gel filtration on Sephadex G-200, and a lower MW of 102,000 was determined by analytical ultracentrifugation. A sedimentation coefficient .**GRAPHIC**. of 5.6S was also determined. A subunit MW of 56,000 was obtained by sodium dodecyl sulfate/polyacrylamide-gel electrophoresis. Isoelectric focusing of sheep kidney extracts indicated the presence of a single band of CoA-transferase activity with pI[isoelectric point]9.0. However, isoelectric focusing of purified CoA-transferase showed the presence of 2 peaks of CoA-transferase activity with pI values of 8.7 and 8.4, suggesting the presence of proteolytic activity during purification. Evidence for sheep kidney CoA-transferase being a dimer of 2 identical subunits was obtained from sodium dodecyl sulfate/polyacrylamide-gel electrophoresis, the amino acid composition, peptide mapping and N-terminal analysis.

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