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Plant Physiology 54:364-367 (1974) © 1974 American Society of Plant Biologists Immunological and Biochemical Studies on Isozymes of Malate Dehydrogenase and Citrate Synthetase in Castor Bean Glyoxysomes 1a Thimann Laboratories, University of California, Santa Cruz, California 95064
Rabbit The glyoxysomal and mitochondrial citrate synthetase from castor bean endosperm show no significant difference in the above immunological test, in their apparent Michaelis constant values for acetyl coenzyme A and oxaloacetate, or in their sensitivity toward ATP inhibition. In the immunological test, glyoxysomal malate dehydrogenase from castor bean endosperm appeared to be related more closely to the leaf peroxisomal malate dehydrogenase from spinach (Spinacia oleracea L.) and to the glyoxysomal malate dehydrogenase from a variety of other fatty seedlings than to the castor bean mitochondrial or soluble malate dehydrogenase. Unlike the mitochondrial or soluble malate dehydrogenase, the castor bean glyoxysomal malate dehydrogenase is easily inactivated by gentle heat treatment, as was reported previously by other workers for the leaf peroxisomal malate dehydrogenase. Thus, the malate dehydrogenases from various plant microbodies share some common characteristics which distinguish them from other isozymes of malate dehydrogenase.
2 Present address: Department of Biology, University of South Carolina, Columbia, S. C. 29208. 1 This work was supported by Grant GB 35376 from the National Science Foundation.
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