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1. The kinetic properties of hybrids of native (or carboxypeptidase-treated) and citraconylated rabbit muscle aldolase are compared with those of equivalent mixtures of the parental enzymes. 2. In the hybrids, the native subunits function slightly less well than in the homotetramer, but the citraconylated subunits have enhanced activity. 3. Subunits of carboxypeptidase-treated aldolase behave essentially as expected in a hybrid environment, but the citraconylated subunits do not show the same enhancement of activity found in the hybrids of native and citraconylated enzyme. The apparent affinity for fructose 1,6-diphosphate of the citraconylated subunits in hybrids of carboxypeptidase-treated and citraconylated aldolase is increased. 4. These results are interpreted in terms of a substrate-induced conformational difference between native and carboxypeptidase-treated aldolase. 5. This conformational change can take place within a single native subunit in the hybrids and does not require a similar conformational change to occur simultaneously in the other three subunits.

Subunit interactions in hybrids of native, carboxypeptidase-treated and citraconylated rabbit muscle aldolase