Effects of univalent cations on the immunoelectrophoretic behavior of pyruvic kinase.

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Abstract
In the presence of univalent cations known to activate pyruvic kinase, one pattern of immunoelectrophoresis (K pattern) was obtained. In the presence of cations that fail to activate the enzyme another pattern (Tris pattern) was observed. These differences in immunoelectrophoretic behavior must reflect differences in the physical organization of the enzyme. The differences are too subtle to be detected by sucrose density gradient centrifugation. Manipulation of the univalent cationic environment results in the reversible interconversion of the immunoelectrophoretic patterns caused by Tris+ or Li+ and by K+. These results are consistent with the reported reversible activation and deactivation of the enzyme by certain univalent cation species. The immunoelectrophoretic behavior of catalase and of sheep serum proteins was not affected differentially by different species of univalent cations indicating that the above kind of observations may be limited to enzymes activated by univalent cations.