Abstract
Ribulose diphosphate carboxylase from many mutant forms of the tomato plant have been studied. Enzymes with altered activity indicative of both high and low specific activity forms have been observed. These enzymes differ in their electrophoretic mobilities and also in their kinetic dependences upon substrate concentrations. Two mutant forms of the enzyme with high specific activity and two with low specific activity have been studied. These ezymes also differ in their ability to bind and to be activated by a protein containing light activating factor.
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