Related Experiment Video
Updated: May 23, 2026

F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes
Published on: May 4, 2013
The function of mitochondrial F(O)F(1) ATP-synthase from the whiteleg shrimp Litopenaeus vannamei muscle during
O Martinez-Cruz1, A M Calderon de la Barca, S Uribe-Carvajal
1Aquatic Molecular Biology Lab. Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6. PO Box. 1735. Hermosillo, Sonora, 83000, Mexico.
Abstract:
The effect of hypoxia and re-oxygenation on the mitochondrial complex F(O)F(1)-ATP synthase was investigated in the whiteleg shrimp Litopenaeus vannamei. A 660 kDa protein complex isolated from mitochondria of the shrimp muscle was identified as the ATP synthase complex. After 10h at hypoxia (1.5-2.0 mg oxygen/L), the concentration of L-lactate in plasma increased significantly, but the ATP amount and the concentration of ATPβ protein remained unaffected. Nevertheless, an increase of 70% in the ATPase activity was detected, suggesting that the enzyme may be regulated at a post-translational level. Thus, during hypoxia shrimp are able to maintain ATP amounts probably by using some other energy sources as phosphoarginine when an acute lack of energy occurs. During re-oxygenation, the ATPase activity decreased significantly and the ATP production continued via the electron transport chain and oxidative phosphorylation. The results obtained showed that shrimp faces hypoxia partially by hydrolyzing the ATP through the reaction catalyzed by the mitochondrial ATPase which increases its activity.
Related Concept Videos
ATP Synthase: Mechanism
ATP Synthase: Structure
Chemiosmosis and ATP Synthesis
Energy Supply for Muscle Contraction
Chemiosmosis
Electron Transport Chain
The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons reduce...
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...

