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Adenosine triphosphatase activity associated with mung bean mitochondria
1Departments of Crop Science and Botany and Crops Research Division, United States Department of Agriculture, North Carolina State University, Raleigh, North Carolina 27607.
Plant Physiology
|April 1, 1971
Summary
Mung bean mitochondria exhibit adenosine triphosphatase activity similar to animal mitochondria. This activity is regulated by specific inhibitors and conditions, revealing insights into plant mitochondrial function.
Area of Science:
- Biochemistry
- Plant Biology
- Mitochondrial Physiology
Background:
- Mitochondria are crucial for cellular energy production in both plants and animals.
- Adenosine triphosphatase (ATPase) activity is a key component of mitochondrial energy metabolism.
Purpose of the Study:
- To characterize the adenosine triphosphatase (ATPase) activity in mung bean mitochondria.
- To compare the properties of mung bean mitochondrial ATPase with those of animal mitochondria.
Main Methods:
- Isolation of tightly coupled, time-stable mung bean mitochondria.
- Assay of adenosine triphosphatase activity under various conditions.
- Investigation of the effects of 2,4-dinitrophenol, oligomycin, oxidizable substrates, sucrose, and Mg(2+) on ATPase activity.
- Analysis of ATPase activity before and after sonication.
Main Results:
- Mung bean mitochondrial ATPase activity closely resembles that of intact animal mitochondria.
- 2,4-Dinitrophenol-induced ATPase activity was inhibited by oligomycin, oxidizable substrates, and high sucrose concentrations.
- Sonication led to high endogenous ATP hydrolysis, requiring Mg(2+), and abolished 2,4-dinitrophenol stimulation and sucrose inhibition, while retaining oligomycin sensitivity.
Conclusions:
- Mung bean mitochondria possess a regulated ATPase system comparable to animal mitochondria.
- The study elucidates the regulatory mechanisms and substrate requirements of plant mitochondrial ATPase.
- Sonication alters the characteristics of mung bean mitochondrial ATPase, highlighting the importance of mitochondrial structural integrity.
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