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Plant Physiology 89:719-723 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Purification and Characterization of Mitochondrial Citrate Synthase

Erica A. Unger1,2 and Aurea C. Vasconcelos

Department of Biological Sciences, Rutgers University, Piscataway, New Jersey 08855-1059

Mitochondrial citrate synthase was purified from leaves of Pisum sativum L. cv Progress 9. A three step purification was employed using ATP-Sepharose affinity chromatography which resulted in a 600-fold enrichment. Enzyme activity was assayed spectrophotometrically during greening of etiolated leaves under constant white light illumination. An increase (1.4 fold) in citrate synthase activity was observed in response to light. Immunoblot analysis of the same samples indicated a constant steady state level of citrate synthase on a per milligram protein basis. These investigations provide supportive evidence for the ability of this trichloroacetic acid cycle enzyme to be active in photosynthesizing tissue.

1 E. A. U. is a recipient of a National Science Foundation (NSF) Predoctoral Graduate Fellowship. Additional support provided by NSF RII 87-03655.

2 Current address: Department of Molecular and Cell Biology, University of Connecticut, U-125, Storrs, CT 06268.




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E. Delhaize, D. M. Hebb, and P. R. Ryan
Expression of a Pseudomonas aeruginosa Citrate Synthase Gene in Tobacco Is Not Associated with Either Enhanced Citrate Accumulation or Efflux
Plant Physiology, April 1, 2001; 125(4): 2059 - 2067.
[Abstract] [Full Text]


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Copyright © 1989 by the American Society of Plant Biologists