Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 68:1406-1408 (1981)
© 1981 American Society of Plant Biologists

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Articles

Metabolism of trans-Aconitic Acid in Maize 1

I. PURIFICATION OF TWO MOLECULAR FORMS OF CITRATE DEHYDRASE

David Brauer and Merle R. Teel

Department of Plant Science, University of Delaware, Newark, Delaware 19711

Trans-aconitate synthesis via citrate dehydrase was determined in crude extracts of maize (Zea mays L.) coleoptiles. Two molecular forms of this enzyme were purified by substrate-specific elution from DEAE-cellulose, ammonium sulfate precipitation, and gel filtration. Each molecular form migrates as a single band in isoelectric focusing. Gel filtration and sodium dodecyl sulfate electrophoresis provided evidence that one enzyme form is composed of four 80,000-dalton subunits while the other is composed of two 60,000-dalton subunits. There was no evidence of proteolytic conversion of the large to the small molecular weight form when the former was incubated with either the 15,000g supernatant or with proteases. The data indicate that the two molecular forms of citrate dehydrase are isozymes.

1 Published with the approval of the Director of the Delaware Agricultural Experiment Station as Miscellaneous Paper No. 901. Contribution No. 116 of the Department of Plant Science, University of Delaware, Newark, DE 19711. This work represents part of the M.S. thesis prepared by D.B.






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Copyright © 1981 by the American Society of Plant Biologists