Linked Life Data

19807066

Source:http://linkedlifedata.com/resource/pubmed/id/19807066

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2009-12-9
pubmed:abstractText
Na(+)-K(+) ATPases have been observed and located by in situ AFM and single molecule recognition technique, topography and recognition imaging (TREC) that is a unique technique to specifically identify single protein in complex during AFM imaging. Na(+)-K(+) ATPases were well distributed in the inner leaflet of cell membranes with about 10% aggregations in total recognized proteins. The height of Na(+)-K(+) ATPases measured by AFM is in the range of 12-14 nm, which is very consistent with the cryoelectron microscopy result. The unbinding force between Na(+)-K(+) ATPases in the membrane and anti-ATPases on the AFM tip is about 80 pN with the apparent loading rate at 40 nN/s. Our results show the first visualization of an essential membrane protein, Na(+)-K(+) ATPase, in quasi-native cell membranes and may be significant to reveal the interactions between Na(+)-K(+) ATPases and other membrane proteins at the molecular level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1530-6992
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4489-93
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Localization of Na+-K+ ATPases in quasi-native cell membranes.
pubmed:affiliation
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't