3‘-0-(4-Benzoyl)benzoyl ATP (BzATP) was synthesized and used as a photoactivatable, covalently binding affinity probe to study site-specific adenine nucleotide binding to the ATPase of submitochondrial particles and the purified soluble F1-ATPase of rat liver mitochondria. In the absence of actinic light, BzATP was a good substrate for enzymic hydrolysis with both soluble and membrane-bound F1-...

3‘-0-(4-Benzoyl)benzoyl ATP (BzATP) was synthesized and used as a photoactivatable, covalently binding affinity probe to study site-specific adenine nucleotide binding to the ATPase of submitochondrial particles and the purified soluble F1-ATPase of rat liver mitochondria. In the absence of actinic light, BzATP was a good substrate for enzymic hydrolysis with both soluble and membrane-bound F1-...

Most P-type ATPases pump specific cations or heavy metals across a membrane to form ion gradients. However, the type IV P-type ATPases evolved the ability to transport specific phospholipid substrates rather than cations and function to establish plasma membrane asymmetry in eukaryotic cells. The mechanism for how a P-type ATPase, or any other transporter, can recognize and flip a phospholipid ...

Ion ATPases in the tissues of aquatic animals are sensitive to metal exposures. Mussels filter-feeding and have a sedentary lifestyle that makes them good bio-indicator animals. Thus, present study was carried out investigate effects copper (0, 30, 90 µg/L) on activities Na-ATPase, Mg-ATPase, Ca-ATPase gill muscle freshwater mussels (Unio tigridis) different exposure durations 7, 14, 21 days). ...

Ruthenium red was found to inhibit actin-activated myosin Mg(2+)-ATPase in smooth muscle and to bind to myosin heavy chain, but not to F-actin. The inhibition by Ruthenium red of actin-activated Mg(2+)-ATPase was of the competitive type with respect to actin (Ki 4.4 microM) and of the non-competitive type with respect to ATP (Ki 6.6 microM). However, Ruthenium red scarcely dissociated the acto-...

A highly conserved amino acid sequence 442GDASE446 in the ATP binding pocket of rat Na/K-ATPase was mutated, and the resulting proteins, G442A, G442P, D443A, S445A, and E446A, were expressed in HeLa cells to investigate the effect of individual ligands on Na/K-ATPase. The apparent Km for the high and low affinity ATP effects was estimated by ATP concentration dependence for the formation of the...