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Plant Physiology 97:1381-1387 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Mitochondrial Malate Dehydrogenase from Corn 1

Purification of Multiple Forms

Marianne K. Hayes, Michael H. Luethy and Thomas E. Elthon

School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0118, Center for Biotechnology, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0118

A method to fractionate corn (Zea mays L. B73) mitochondria into soluble proteins, high molecular weight soluble proteins, and membrane proteins was developed. These fractions were analyzed by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and assays of mitochondrial enzyme activities. The Krebs cycle enzymes were enriched in the soluble fraction. Malate dehydrogenase has been purified from the soluble fraction by a two-step fast protein liquid chromatography method. Six different malate dehydrogenase peaks were obtained from the Mono Q column. These peaks were individually purified using a Phenyl Superose column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified peaks showed that three of the isoenzymes consisted of different homodimers (I, III, VI) and three were different heterodimers (II, IV, V). Apparent molecular masses of the three different monomer subunits were 37, 38, and 39 kilodaltons. Nondenaturing gel analysis of the malate dehydrogenase peaks showed that each Mono Q peak contained a band of malate dehydrogenase activity with different mobility. These observations are consistent with three nuclear genes encoding corn mitochondrial malate dehydrogenase. Polyclonal antibodies raised against purified malate dehydrogenase were used to identify the gene products using Western blots of two-dimensional gels.

1 This work was supported by the Center for Biotechnology, University of Nebraska-Lincoln.




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