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Biochimie|August 8, 2006
CadA, the Cd2+-ATPase from Listeria monocytogenes, can use Cd2+ as co-substrateC C Wu, A Gardarin, P Catty, et al.European Journal of Biochemistry|August 15, 1991
Ca2+ gradient and drugs reveal different binding sites for Pi and Mg2+ in phosphorylation of the sarcoplasmic reticulum ATPaseL De Meis, V A Suzano, T Caldeira, et al.Biochemistry|November 18, 1986
Rapid filtration study of the phosphorylation-dependent dissociation of calcium from transport sites of purified sarcoplasmic reticulum ATPase and ATP modulation of the catalytic cycleP Champeil, F GuillainThe Journal of Biological Chemistry|May 25, 1990
Reaction mechanism of Ca2+ ATPase of sarcoplasmic reticulum. Equilibrium and transient study of phosphorylation with Ca.ATP as substrateJ J Lacapere, F GuillainEuropean Journal of Biochemistry|January 15, 1993
The reaction mechanism of Ca(2+)-ATPase of sarcoplasmic reticulum. Direct measurement of the Mg.ATP dissociation constant gives similar values in the presence or absence of calciumJ J Lacapere, F GuillainBiochemistry|March 17, 1981
Pressure-induced inactivation of sarcoplasmic reticulum adenosine triphosphatase during high-speed centrifugationP Champeil, S Büschlen, F GuillainBiochemistry|September 25, 1984
Sarcoplasmic reticulum adenosinetriphosphatase phosphorylation from inorganic phosphate. Theoretical and experimental reinvestigationF Guillain, P Champeil, P D BoyerIssue Brief (Health Policy Tracking Service)|November 10, 2000
Providers issue brief: certificate of needE MintzThe Journal of Biological Chemistry|July 10, 1982
Direct fluorescence measurements of Mg2+ binding to sarcoplasmic reticulum ATPaseF Guillain, M P Gingold, P ChampeilIssue Brief (Health Policy Tracking Service)|November 10, 2000
Providers issue brief: certificate of needE MintzPageof 7