Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Barry J.R. Pitts"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 483:294-302
1. 1.|Calcium binding to (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) preparations from beef and pig heart preparations of varying degrees of purity was measured. 2. 2.|Binding was inhibited by Mg2+, Na+ and K+. Inhibition by Na+ and K+ appea
Autor:
Barry J.R. Pitts, Laurence R. Meyerson
Publikováno v:
Drug Development Research. 1:43-49
Sanguinarine, an isoquinoline alkaloid belonging to the benzophenanthridine class, has been found to be a time-dependent inhibitor of cardiac Na,K-ATPase activity. Enzyme inhibition depended on the concentration of enzyme in the assay. Dilution and c
Autor:
Barry J.R. Pitts
Publikováno v:
Annals of the New York Academy of Sciences. 242:293-304
Autor:
Arnold Schwartz, Jeanie M. Wood, Earl T. Wallick, Barry J.R. Pitts, Robert J. Adams, Oscar A. Gende
Publikováno v:
Journal of Molecular and Cellular Cardiology. 11:941-959
Palmitylcarnitine, an endogenous long-chain fatty acyl ester, inhibited cardiac Na, K-ATPase activity and binding of [ 3 H]ouabain to the enzyme. The inhibitory effects on enzyme hydrolytic activity and drug binding were time and concentration depend
Publikováno v:
Biochemical Journal. 210:339-344
To determine the neural influence on the function of the sarcoplasmic reticulum (SR) of fast-twitch skeletal muscle, the superior pectoralis muscle of adult chicken was denervated, and the SR was isolated at 20 days post-denervation. The isolated SR
Publikováno v:
Biochemical Pharmacology. 38:3331-3339
In this study three forms of cyclic nucleotide phosphodiesterase (PDE) isolated from rabbit aorta were pharmacologically characterized, and the consequence of selective inhibition of calmodulin-stimulated PDE (CaM-PDE) and cGMP specific PDE (cG-PDE)
Autor:
Arnold Schwartz, Barry J.R. Pitts
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 401:184-195
A method is described for purification of (N + , K + )-ATPase which yields approximately 60 mg of enzyme from 800 g of cardiac muscle with specific activities ranging from 340 to 400 μmol inorganic phosphate/mg protein per h (units/mg). Sodium dodec
Publikováno v:
Biochemical Pharmacology. 22:9-15
The effects of ascorbate and dehydroascorbate on the Na+, K+-adenosine triphosphatase (ATPase) preparations of several tissues were studied. Both compounds inhibited the ATPase activities of the preparations obtained from the brains of rat, guinea pi
Autor:
Amir Askari, Barry J.R. Pitts
Publikováno v:
Archives of Biochemistry and Biophysics. 154:476-482
Ouabain activation of the phosphatase associated with Na + ,K + -ATPase is a time-dependent process which is stimulated by ATP and other nucleotides. Further stimulation by Na + is observed under certain conditions. The stimulatory effect of ATP was
Publikováno v:
Journal of Biological Chemistry. 253:8671-8673
A pure, enzymatically active Ca2+-dependent adenosine triphosphatase (Ca2+-ATPase) has been isolated from canine ventricular sarcoplasmic reticulum. In contrast to that derived from skeletal muscle, the Ca2+-ATPase from cardiac sarcoplasmic reticulum