Abstract
Crystalline pig heart fumarase was found to be highly heterogeneous by gel electrophoresis and ion-exchange chromatography. The enzyme was resolved into five active components by chromatography. These components in turn appear heterogeneous; one yielded four electrophoretic bands. Each chromatographic component has the same molecular weight as the original sample; contains four subunits of molwt 48,500; retains its particular chromatographic behavior on rechromatography; can be reconverted to active enzyme after urea dissociation of subunits. Each chromatographic component yielded three or four chromatographic peaks after dissociation and reassociation, but no two yielded the same pattern, showing that there are differences in primary structure between the subunits. The data are consistent with the presence of at least three different subunit types.
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