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Plant Physiology 82:664-670 (1986)
© 1986 American Society of Plant Biologists

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Articles

Purification and Properties of Hypoxically Induced Lactate Dehydrogenase from Barley Roots 1

Neil E. Hoffman2 and Andrew D. Hanson

MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824

Using Affigel Blue and oxamate-agarose affinity chromatography, lactate dehydrogenase (LDH) was purified 2000-fold from hypoxically induced barley roots. Molecular weights of the native and sodium dodecyl sulfate-denatured LDH protein were 157 and 40 kilodaltons, respectively, indicating a tetramer. Purified barley LDH was very similar in size and kinetic properties to potato LDH. However, their amino acid compositions differed substantially and antibodies raised against barley LDH did not cross-react with potato LDH on immunoblots, implying that the barley and potato LDHs are not closely related proteins. In vivo [35S] methionine labeling and immunoprecipitation experiments indicated that hypoxia increased the rate of LDH protein synthesis, and immunoblot analysis showed that LDH protein levels rose during hypoxia. We conclude that increased enzyme synthesis plays a major part in the induction of LDH enzyme activity by low O2 levels in barley roots.

2 Present address: Laboratory of Cell Biology, Rockefeller University, New York, NY 10021.

1 Research conducted under contract DE-AC02-76ERO-1338 from the United States Department of Energy. Michigan Agricultural Experiment Journal Article 11915.






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Copyright © 1986 by the American Society of Plant Biologists