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Plant Physiology 77:339-345 (1985) © 1985 American Society of Plant Biologists Isolation and Antigenic Characterization of Corn Mitochondrial F1-ATPase 1Plant Breeding and Biometry, Cornell University, Ithaca, New York, Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588-0304, School of Biological Sciences, University of Nebraska, Lincoln, Nebraska 68588-0304
Corn mitochondrial F1-ATPase was purified from submitochondrial particles by chloroform extraction. Enzyme stored in ammonium sulfate at 4°C was substantially activated by ATP, while enzyme stored at 70°C in 25% glycerol was not. Enzyme in glycerol remained fully active (8-9 micromoles Pi released per minute per milligram), while the ammonium sulfate preparations steadily lost activity over a 2-month storage period. The enzyme was cold labile, and inactived by 4 minutes at 60°C. Treatment with octylglucoside resulted in complete loss of activity, while vanadate had no effect on activity. The apparent subunit molecular weights of corn mitochondrial F1-ATPase were determined by SDS-polyacrylamide gel electrophoresis to be 58,000 (
1 N. P. was supported by National Institutes of Health, National Research Service Award CA 07420 from the National Cancer Institute. V. S. was supported by National Science Foundation Grant PCM-8341774. S. M. S. acknowledges support from the National Science Foundation Grant PCM 84-09287, as well as a Research Career Development Award from the National Cancer Institute (CA 00628) of the Department of Health and Human Services.
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