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Related Experiment Videos

Oligomycin-sensitive ATPase of Submitochondrial Particles from Corn.

C Grubmeyer1, M Spencer

  • 1Department of Plant Science, University of Alberta, Edmonton, Alberta, Canada T6G 2E3.

Plant Physiology
|April 1, 1978
PubMed
Summary

Corn mitochondria contain a unique cold-stable ATPase. This enzyme, unlike others, is not inhibited by oligomycin, suggesting novel functions in plant energy metabolism.

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Area of Science:

  • Plant Physiology
  • Mitochondrial Biochemistry
  • Enzyme Activity

Background:

  • Monocotyledons were hypothesized to possess a unique oligomycin-insensitive ATPase.
  • Previous research on ATPases from various organisms provided a basis for comparison.
  • Understanding plant mitochondrial ATPases is crucial for energy metabolism studies.

Purpose of the Study:

  • To investigate the presence and characteristics of a unique ATPase in corn (Zea mays L.) mitochondria.
  • To determine the sensitivity of corn mitochondrial ATPase activity to oligomycin.
  • To characterize the properties of submitochondrial particles and soluble fractions from corn mitochondria.

Main Methods:

  • Preparation of submitochondrial particles and soluble fractions from sonicated corn mitochondria.

Related Experiment Videos

  • Assay of ATPase activity in different fractions.
  • Testing the effects of oligomycin, azide, trypsin, and sodium chloride on ATPase activity.
  • Evaluation of the cold-stability of the soluble ATPase fraction.

    • Main Results:

    • Corn submitochondrial particles exhibited ATPase activity that was sensitive to oligomycin and activated by trypsin, similar to ATPases from other sources.
    • A soluble fraction from corn mitochondria contained an active ATPase inhibited by azide and stimulated by sodium chloride and trypsin.
    • This soluble ATPase fraction demonstrated cold-stability, a characteristic not typically observed in other F(1)-ATPases.

    Conclusions:

    • The hypothesis of a unique oligomycin-insensitive ATPase in monocotyledons was not supported by the study of corn mitochondria.
    • Corn mitochondria possess both oligomycin-sensitive and cold-stable ATPase activities, indicating distinct enzymatic components.
    • The cold-stable soluble ATPase from corn may represent a novel enzyme with unique properties and functions in plant energy regulation.