Linked Life Data

15121095

Source:http://linkedlifedata.com/resource/pubmed/id/15121095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-5-3
pubmed:abstractText
The red cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and mediates the stilbene-disulfonate-sensitive, electroneutral exchange of chloride and bicarbonate. Previous studies showed that the integrity of the third extracellular loop (EC3) of the protein was not essential for stilbene-disulfonate-sensitive chloride uptake. Here we demonstrate that the chloride uptake mediated by assemblies separated at EC3 represents the physiological electroneutral Cl(-)/HCO(3)(-) activity associated with intact AE1 protein. This provides further evidence that the 1:5 and 6:14 regions of the protein form discrete folding domains and confirms that the third extracellular loop does not play a pivotal role in AE1 transport function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1079-9796
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The disruption of the third extracellular loop of the red cell anion exchanger AE1 does not affect electroneutral Cl-/HCO3- exchange activity.
pubmed:affiliation
Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK. mark.parker@yale.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't