Abstract
Malate synthetase was purified over 200-fold from maize scutella. Catalase remains associated with malate synthetase during most of the purification procedure. The two enzymes can be separated by gel filtration on Sepharose 6B. The molecular weight of malate synthetase as estimated by gel filtration and density gradient sedimentation is approximately 500 000. 5.6 m M ATP causes a 57.5% inhibition of the enzymatic activity. The inhibition is competitive with respect to acetylcoenzyme A. ADP and AMP have a smaller inhibitory effect.
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