rdf:type |
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0022023,
umls-concept:C0205119,
umls-concept:C0456962,
umls-concept:C0596902,
umls-concept:C0597694,
umls-concept:C0872303,
umls-concept:C0936012,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C2003851
|
pubmed:issue |
1
|
pubmed:dateCreated |
2005-6-29
|
pubmed:abstractText |
We present a procedure for determination of 11 system parameters of an ion transporter expressed in Xenopus oocytes. The experiments consist of fast triangular voltage-clamp experiments in the presence and absence of external substrate. A four-state enzymatic cycle operating between an external and an internal section of electrodiffusion is used for analysis. The explicit example treats experiments with the fungal 2H+-NO3- symporter EnNRT, a member of the major superfamily transporters. The results comprise a density of approximately 150 fmol functional transporter molecules per oocyte, a gross charge number z(E) approximately -0.3 of the empty binding site of the enzyme, individual rate constants for reorientation of the empty and occupied binding site in the range of 5-500 s(-1), electrical access sections between bulk solutions and reaction cycle of approximately 3% inside and 15% outside, an increase of internal NO3- at the plasma membrane from approximately 0.5 to approximately 2 mM during exposure to external NO3-, and K(D) approximately 0.3 microM3 inside and K(D) approximately 3 microM3 outside in binding the triplicate substrate (2H+ +NO3-). The results compare well with the known structure of the lactose permease, another major superfamily transporter.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-10541797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-10811976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-10984478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-11279252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-11689935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-11689945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-11867451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-12691752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-12893932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-1382188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-14692450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-14762704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-1986367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-2435332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-3225842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-6162960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-68708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-7310856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-8035166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-8189208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-8382257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-9533718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15849255-9834140
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0006-3495
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
89
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
734-44
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:15849255-Animals,
pubmed-meshheading:15849255-Binding Sites,
pubmed-meshheading:15849255-Biological Transport,
pubmed-meshheading:15849255-Biophysics,
pubmed-meshheading:15849255-Carrier Proteins,
pubmed-meshheading:15849255-Cell Membrane,
pubmed-meshheading:15849255-Diffusion,
pubmed-meshheading:15849255-Dose-Response Relationship, Drug,
pubmed-meshheading:15849255-Electrophysiology,
pubmed-meshheading:15849255-Ions,
pubmed-meshheading:15849255-Kinetics,
pubmed-meshheading:15849255-Membrane Transport Proteins,
pubmed-meshheading:15849255-Oocytes,
pubmed-meshheading:15849255-Patch-Clamp Techniques,
pubmed-meshheading:15849255-Symporters,
pubmed-meshheading:15849255-Time Factors,
pubmed-meshheading:15849255-Xenopus
|
pubmed:year |
2005
|
pubmed:articleTitle |
Fast, triangular voltage clamp for recording and kinetic analysis of an ion transporter expressed in Xenopus oocytes.
|
pubmed:affiliation |
Abteilung Biophysik der Pflanze der Universität, Untere Karspüle 2, 37073 Göttingen, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|