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10.1085/jgp.112.5.549 http://scihub22266oqcxt.onion/10.1085/jgp.112.5.549 9806964!2229443!9806964     free     free     free 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 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 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Gen+Physiol 1998 ; 112 (5): 549-58 Nephropedia Template TP {{tp|p=9806964|t=1998. Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding |pdf=|usr=}}{{9806964}} gab.com Text Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding JO: J Gen Physiol http://www.kidney.de/pget.php?&tw=1&pmid=9806964 #FOAvip The human and shark Na-K-Cl cotransporters (NKCCs) are 74% identical in amino acid sequence yet they display marked differences in apparent affinities for the ions and bumetanide. In this study, we have used chimeras and point mutations to determine which transmembrane domains (tm's) are responsible for the differences in ion transport and in inhibitor binding kinetics. When expressed in HEK-293 cells, all the mutants carry out bumetanide-sensitive 86Rb influx. The kinetic behavior of these constructs demonstrates that the first seven tm's contain all of the residues conferring affinity differences. In conjunction with our previous finding that tm 2 plays an important role in cation transport, the present observations implicate the fourth and seventh tm helices in anion transport. Thus, it appears that tm's 2, 4, and 7 contain the essential affinity-modifying residues accounting for the human-shark differences with regard to cation and anion transport. Point mutations have narrowed the list of candidates to 13 residues within the three tm's. The affinity for bumetanide was found to be affected by residues in the same tm 2-7 region, and also by residues in tm's 11 and 12. Unlike for the ions, changes in bumetanide affinity were nonlinear and difficult to interpret: the Ki(bumetanide) of a number of the constructs was outside the range of sNKCC1 and hNKCC1 Kis. Twit Text FOAVip Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding ????J Gen Physiol http://www.kidney.de/pget.php?&tw=1&pmid=9806964 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=9806964 #FOAvip English Wikipedia <ref>{{Cite pmid|9806964}}</ref> Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding #MMPMID9806964 Isenring P; Jacoby SC; Chang J; Forbush B J Gen Physiol 1998[Nov]; 112 (5): 549-58 PMID9806964show ga The human and shark Na-K-Cl cotransporters (NKCCs) are 74% identical in amino acid sequence yet they display marked differences in apparent affinities for the ions and bumetanide. In this study, we have used chimeras and point mutations to determine which transmembrane domains (tm's) are responsible for the differences in ion transport and in inhibitor binding kinetics. When expressed in HEK-293 cells, all the mutants carry out bumetanide-sensitive 86Rb influx. The kinetic behavior of these constructs demonstrates that the first seven tm's contain all of the residues conferring affinity differences. In conjunction with our previous finding that tm 2 plays an important role in cation transport, the present observations implicate the fourth and seventh tm helices in anion transport. Thus, it appears that tm's 2, 4, and 7 contain the essential affinity-modifying residues accounting for the human-shark differences with regard to cation and anion transport. Point mutations have narrowed the list of candidates to 13 residues within the three tm's. The affinity for bumetanide was found to be affected by residues in the same tm 2-7 region, and also by residues in tm's 11 and 12. Unlike for the ions, changes in bumetanide affinity were nonlinear and difficult to interpret: the Ki(bumetanide) of a number of the constructs was outside the range of sNKCC1 and hNKCC1 Kis. |Animals[MESH] |Binding Sites/physiology[MESH] |Bumetanide/metabolism/*pharmacology[MESH] |Carrier Proteins/*chemistry/*genetics/metabolism[MESH] |Cells, Cultured[MESH] |Chlorides/metabolism[MESH] |Diuretics/metabolism/*pharmacology[MESH] |Humans[MESH] |Kidney/cytology[MESH] |Kinetics[MESH] |Mutagenesis, Site-Directed/physiology[MESH] |Oligonucleotide Probes[MESH] |Potassium/metabolism[MESH] |Protein Structure, Tertiary[MESH] |Recombinant Fusion Proteins/genetics/metabolism[MESH] |Rubidium Radioisotopes[MESH] |Sharks[MESH] |Sodium-Potassium-Chloride Symporters[MESH] |Sodium/metabolism[MESH]Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in(epmc).pdf DeepDyve Pubget Overpricing