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http://scihub22266oqcxt.onion/ 10362846!ä!10362846 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 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Exp+Physiol 1999 ; 84 (3): 471-88 Nephropedia Template TP {{tp|p=10362846|t=1999. Effect of extracellular cations on the inward rectifying K+ channels Kir2 1 and Kir3 1/Kir3 4 |pdf=|usr=}}{{10362846}} gab.com Text Effect of extracellular cations on the inward rectifying K+ channels Kir2 1 and Kir3 1/Kir3 4 JO: Exp Physiol http://www.kidney.de/pget.php?&tw=1&pmid=10362846 #FOAvip The effects of Ba2+, Mg2+, Ca2+ and Na+ as blocking ions were investigated in 90 and 10 mM extracellular K+ solutions on the cloned inward rectifying K+ channel Kir2.1 expressed in Xenopus oocytes. Some data were also obtained using another inward rectifying K+ channel Kir3.1/Kir3.4. The addition of Ba2+ caused a concentration-, voltage- and time-dependent block of both channels. Decreasing the extracellular K+ concentration augmented the block. The data suggest that Ba2+ blocks the channels by binding to a site within the channel pore and that the electrical binding distance, delta, of the site is significantly different for Kir2.1 and Kir3. 1/Kir3.4 (0.38 and 0.22, respectively). Mg2+ and Ca2+ caused an instantaneous concentration- and voltage-dependent block of both channels. With Kir2.1, decreasing the K+ concentration augmented the block. The voltage dependence of the block was less than that of Ba2+ ([delta], 0.1), indicating a more superficial binding site for these ions within the channel pore. The affinity of the channels for Mg2+ and Ca2+ was 1000-fold lower than that for Ba2+. Addition of Na+ resulted in a concentration-, voltage- and time-dependent block of Kir2.1, similar to that observed with Ba2+. The competition between the blocking cations (for Kir2.1: Ba2+, Mg2+, Ca2+; for Kir3. 1/Kir3.4: Ba2+) and extracellular K+ suggests that the binding sites for the blocking cations may be sites to which K+ binds as part of the normal passage of K+ through the channels. It is possible that under normal physiological conditions naturally occurring extracellular cations may partly block the two inward rectifying K+ channels. Twit Text FOAVip Effect of extracellular cations on the inward rectifying K+ channels Kir2 1 and Kir3 1/Kir3 4 ????Exp Physiol http://www.kidney.de/pget.php?&tw=1&pmid=10362846 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=10362846 #FOAvip English Wikipedia <ref>{{Cite pmid|10362846}}</ref> Effect of extracellular cations on the inward rectifying K+ channels Kir2 1 and Kir3 1/Kir3 4 #MMPMID10362846 Owen JM; Quinn CC; Leach R; Findlay JB; Boyett MR Exp Physiol 1999[May]; 84 (3): 471-88 PMID10362846show ga The effects of Ba2+, Mg2+, Ca2+ and Na+ as blocking ions were investigated in 90 and 10 mM extracellular K+ solutions on the cloned inward rectifying K+ channel Kir2.1 expressed in Xenopus oocytes. Some data were also obtained using another inward rectifying K+ channel Kir3.1/Kir3.4. The addition of Ba2+ caused a concentration-, voltage- and time-dependent block of both channels. Decreasing the extracellular K+ concentration augmented the block. The data suggest that Ba2+ blocks the channels by binding to a site within the channel pore and that the electrical binding distance, delta, of the site is significantly different for Kir2.1 and Kir3. 1/Kir3.4 (0.38 and 0.22, respectively). Mg2+ and Ca2+ caused an instantaneous concentration- and voltage-dependent block of both channels. With Kir2.1, decreasing the K+ concentration augmented the block. The voltage dependence of the block was less than that of Ba2+ ([delta], 0.1), indicating a more superficial binding site for these ions within the channel pore. The affinity of the channels for Mg2+ and Ca2+ was 1000-fold lower than that for Ba2+. Addition of Na+ resulted in a concentration-, voltage- and time-dependent block of Kir2.1, similar to that observed with Ba2+. The competition between the blocking cations (for Kir2.1: Ba2+, Mg2+, Ca2+; for Kir3. 1/Kir3.4: Ba2+) and extracellular K+ suggests that the binding sites for the blocking cations may be sites to which K+ binds as part of the normal passage of K+ through the channels. It is possible that under normal physiological conditions naturally occurring extracellular cations may partly block the two inward rectifying K+ channels. |*Potassium Channels, Inwardly Rectifying[MESH] |Animals[MESH] |Barium/pharmacology[MESH] |Binding Sites[MESH] |Calcium/pharmacology[MESH] |Cations/pharmacology[MESH] |Female[MESH] |G Protein-Coupled Inwardly-Rectifying Potassium Channels[MESH] |Humans[MESH] |In Vitro Techniques[MESH] |Kinetics[MESH] |Magnesium/pharmacology[MESH] |Oocytes/metabolism[MESH] |Potassium Channels/genetics/*metabolism[MESH] |Recombinant Proteins/genetics/metabolism[MESH] |Sodium/pharmacology[MESH]Effect of extracellular cations on the inward rectifying K+ channels K(epmc).pdf DeepDyve Pubget Overpricing