Linked Life Data

20875821

Source:http://linkedlifedata.com/resource/pubmed/id/20875821

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2010-10-18
pubmed:abstractText
Soybean nodulin 26 (nod26), a member of the aquaporin superfamily, is the major protein component of the symbiosome membrane that encloses nitrogen-fixing bacteroids in root nodules. Previous work has demonstrated that nod26 facilitates the transport of water and glycerol, although a potential additional role as a channel for fixed ammonia efflux has been hypothesized. In the present study it is shown that recombinant nod26 reconstituted into proteoliposomes facilitates NH(3) transport in an Hg(2+)-sensitive manner with a reduced activation energy, hallmarks of protein-facilitated transport characteristic of aquaporins. Comparison of the predicted single-channel transport rates of nod26 suggests a 4.9-fold preference for ammonia compared to water.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1873-3468
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
584
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4339-43
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Ammonia permeability of the soybean nodulin 26 channel.
pubmed:affiliation
Graduate School of Genome Science and Technology, The University of Tennessee-Oak Ridge National Laboratory, Oak Ridge, TN 37830, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.