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http://scihub22266oqcxt.onion/ 11201505!ä!11201505 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Can+J+Physiol+Pharmacol 2001 ; 79 (1): 8-12 Nephropedia Template TP {{tp|p=11201505|t=2001. Evidence for the binding of beta-adrenoceptor blockers to microsomal Na+/K+-ATPase in guinea pig heart preparations |pdf=|usr=}}{{11201505}} gab.com Text Evidence for the binding of beta-adrenoceptor blockers to microsomal Na+/K+-ATPase in guinea pig heart preparations JO: Can J Physiol Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=11201505 #FOAvip We reported in a previous study that beta-adrenoceptor blockers inhibit the Mg2+-dependent ATP-hydrolytic function of Na+/K+-ATPase. To determine if this action is a result of binding of beta-blockers to the receptor sites that bind the digitalis glycosides, we performed displacement binding assays of eight beta-blockers with [3H]-ouabain (OUA) in guinea pig myocardial microsomal preparations. In the first series of experiments, 10-200 microM of the beta-blockers were displaced with 250 nM OUA. In the second set of experiments, 10-500 nM of OUA was displaced using 200 microM of the beta-blockers. The drugs showed concentration-dependent receptor occupancy at the different OUA levels. Propranolol (PPN), metoprolol (MTP), and sotalol (STL) showed the strongest binding; nadolol (NDL), indenolol (IDN), and atenolol (ATN) had intermediate binding; carazolol (CRZ) and celiprolol (CLP) had the weakest binding properties. The results suggest that beta-blockers may compete for the same binding sites with ouabain in their inhibition of the Na+/K+-ATPase. These actions may contribute to the mechanism for some of their cardiac effects, especially their proarrhythmic and arrhythmogenic actions. Twit Text FOAVip Evidence for the binding of beta-adrenoceptor blockers to microsomal Na+/K+-ATPase in guinea pig heart preparations ????Can J Physiol Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=11201505 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=11201505 #FOAvip English Wikipedia <ref>{{Cite pmid|11201505}}</ref> Evidence for the binding of beta-adrenoceptor blockers to microsomal Na+/K+-ATPase in guinea pig heart preparations #MMPMID11201505 Almotrefi AA; Basco C; Moorji A; Dzimiri N Can J Physiol Pharmacol 2001[Jan]; 79 (1): 8-12 PMID11201505show ga We reported in a previous study that beta-adrenoceptor blockers inhibit the Mg2+-dependent ATP-hydrolytic function of Na+/K+-ATPase. To determine if this action is a result of binding of beta-blockers to the receptor sites that bind the digitalis glycosides, we performed displacement binding assays of eight beta-blockers with [3H]-ouabain (OUA) in guinea pig myocardial microsomal preparations. In the first series of experiments, 10-200 microM of the beta-blockers were displaced with 250 nM OUA. In the second set of experiments, 10-500 nM of OUA was displaced using 200 microM of the beta-blockers. The drugs showed concentration-dependent receptor occupancy at the different OUA levels. Propranolol (PPN), metoprolol (MTP), and sotalol (STL) showed the strongest binding; nadolol (NDL), indenolol (IDN), and atenolol (ATN) had intermediate binding; carazolol (CRZ) and celiprolol (CLP) had the weakest binding properties. The results suggest that beta-blockers may compete for the same binding sites with ouabain in their inhibition of the Na+/K+-ATPase. These actions may contribute to the mechanism for some of their cardiac effects, especially their proarrhythmic and arrhythmogenic actions. |Adrenergic beta-Antagonists/*metabolism[MESH] |Animals[MESH] |Binding, Competitive/drug effects[MESH] |Guinea Pigs[MESH] |In Vitro Techniques[MESH] |Male[MESH] |Microsomes/enzymology/*metabolism[MESH] |Myocardium/*enzymology[MESH] |Ouabain/metabolism[MESH]Evidence for the binding of beta-adrenoceptor blockers to microsomal (epmc).pdf DeepDyve Pubget Overpricing