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10.1152/ajpcell.1998.275.4.C995 http://scihub22266oqcxt.onion/10.1152/ajpcell.1998.275.4.C995 9755053!ä!9755053 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Physiol 1998 ; 275 (4): C995-C1008 Nephropedia Template TP {{tp|p=9755053|t=1998. Characterization of two Mg2+ transporters in sealed plasma membrane vesicles from rat liver |pdf=|usr=}}{{9755053}} gab.com Text Characterization of two Mg2+ transporters in sealed plasma membrane vesicles from rat liver JO: Am J Physiol http://www.kidney.de/pget.php?&tw=1&pmid=9755053 #FOAvip The plasma membrane of mammalian cells possesses rapid Mg2+ transport mechanisms. The identity of Mg2+ transporters is unknown, and so are their properties. In this study, Mg2+ transporters were characterized using a biochemically and morphologically standardized preparation of sealed rat liver plasma membranes (LPM) whose intravesicular content could be set and controlled. The system has the advantages that it is not regulated by intracellular signaling machinery and that the intravesicular ion milieu can be designed. The results indicate that 1) LPM retain trapped intravesicular total Mg2+ with negligible leak; 2) the addition of Na+ or Ca2+ induces a concentration- and temperature-dependent efflux corresponding to 30-50% of the intravesicular Mg2+; 3) the rate of flux is very rapid (137.6 and 86.8 nmol total Mg2+ . micrometer -2 . min-1 after Na+ and Ca2+ addition, respectively); 4) coaddition of maximal concentrations of Na+ and Ca2+ induces an additive Mg2+ efflux; 5) both Na+- and Ca2+-stimulated Mg2+ effluxes are inhibited by amiloride, imipramine, or quinidine but not by vanadate or Ca2+ channel blockers; 6) extracellular Na+ or Ca2+ can stimulate Mg2+ efflux in the absence of Mg2+ gradients; and 7) Mg2+ uptake occurs in LPM loaded with Na+ but not with Ca2+, thus indicating that Na+/Mg2+ but not Ca2+/Mg2+ exchange is reversible. These data are consistent with the operation of two distinct Mg2+ transport mechanisms and provide new information on rates of Mg2+ transport, specificity of the cotransported ions, and reversibility of the transport. Twit Text FOAVip Characterization of two Mg2+ transporters in sealed plasma membrane vesicles from rat liver ????Am J Physiol http://www.kidney.de/pget.php?&tw=1&pmid=9755053 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=9755053 #FOAvip English Wikipedia <ref>{{Cite pmid|9755053}}</ref> Characterization of two Mg2+ transporters in sealed plasma membrane vesicles from rat liver #MMPMID9755053 Cefaratti C; Romani A; Scarpa A Am J Physiol 1998[Oct]; 275 (4): C995-C1008 PMID9755053show ga The plasma membrane of mammalian cells possesses rapid Mg2+ transport mechanisms. The identity of Mg2+ transporters is unknown, and so are their properties. In this study, Mg2+ transporters were characterized using a biochemically and morphologically standardized preparation of sealed rat liver plasma membranes (LPM) whose intravesicular content could be set and controlled. The system has the advantages that it is not regulated by intracellular signaling machinery and that the intravesicular ion milieu can be designed. The results indicate that 1) LPM retain trapped intravesicular total Mg2+ with negligible leak; 2) the addition of Na+ or Ca2+ induces a concentration- and temperature-dependent efflux corresponding to 30-50% of the intravesicular Mg2+; 3) the rate of flux is very rapid (137.6 and 86.8 nmol total Mg2+ . micrometer -2 . min-1 after Na+ and Ca2+ addition, respectively); 4) coaddition of maximal concentrations of Na+ and Ca2+ induces an additive Mg2+ efflux; 5) both Na+- and Ca2+-stimulated Mg2+ effluxes are inhibited by amiloride, imipramine, or quinidine but not by vanadate or Ca2+ channel blockers; 6) extracellular Na+ or Ca2+ can stimulate Mg2+ efflux in the absence of Mg2+ gradients; and 7) Mg2+ uptake occurs in LPM loaded with Na+ but not with Ca2+, thus indicating that Na+/Mg2+ but not Ca2+/Mg2+ exchange is reversible. These data are consistent with the operation of two distinct Mg2+ transport mechanisms and provide new information on rates of Mg2+ transport, specificity of the cotransported ions, and reversibility of the transport. |Animals[MESH] |Antiporters/isolation & purification/*metabolism[MESH] |Biological Transport[MESH] |Calcimycin/pharmacology[MESH] |Cation Transport Proteins[MESH] |Cations, Divalent/pharmacology[MESH] |Cell Fractionation[MESH] |Cell Membrane/*metabolism/ultrastructure[MESH] |Centrifugation, Density Gradient[MESH] |Kinetics[MESH] |Liver/*metabolism[MESH] |Magnesium/*metabolism[MESH] |Male[MESH] |Microscopy, Electron[MESH] |Ouabain/metabolism[MESH] |Rats[MESH]Characterization of two Mg2+ transporters in sealed plasma membrane ve(epmc).pdf DeepDyve Pubget Overpricing