The ATPase activity of Jerusalem-artichoke mitochondria and submitochondrial particles
Review articleOpen access
Abstract:

Abstract1.1. Some properties of the ATPase activity of Jerusalem-artichoke mitochondria and submitochondrial particles are described.2.2. Intact mitochondria catalyse a slow rate of hydrolysis of ATP, which is only slightly enhanced by the addition of uncouplers, but which is sensitive to oligomycin.3.3. Succinate stimulates the rate of hydrolysis of ATP by intact mitochondria but this stimulation is insensitive to oligomycin, and may not therefore involve the classical mitochondrial ATPase (F1).4.4. Broken mitochondria or sonically-prepared submitochondrial particles catalyse a rapid hydrolysis of ATP in the absence of uncoupler which is strongly inhibited by oligomycin.5.5. The ATPase of submitochondrial particles is specific for adenine nucleotides.6.6. These findings indicate that breakage of the mitochondrial membrane may increase the accessibility of the F1-ATPase to ATP without losing the substrate specificity.

Request full text

References (0)

Cited By (0)

No reference data.
No citation data.
Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!