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. 1985 Feb;77(2):339–345. doi: 10.1104/pp.77.2.339

Isolation and Antigenic Characterization of Corn Mitochondrial F1-ATPase 1

Vitaly L Spitsberg 1,2,3, Nancy E Pfeiffer 1,2,3, Bruce Partridge 1,2,3, Dwane E Wylie 1,2,3, Sheldon M Schuster 1,2,3
PMCID: PMC1064516  PMID: 16664055

Abstract

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 (α), 55,000 (β), 35,000 (γ), 22,000 (δ), and 12,000 (ε). Monoclonal and polyclonal antibodies used in competitive binding assays demonstrated that corn mitochondrial F1-ATPase was antigenically distinct from the chloroplastic CF1-ATPases of corn and spinach. Monoclonal antibodies against antigenic sites on spinach CF1-ATPase β and γ subunits were used to demonstrate that those sites were either changed substantially or totally absent from the mitochondrial F1-ATPase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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