Linked Life Data

2476185

Source:http://linkedlifedata.com/resource/pubmed/id/2476185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-10-13
pubmed:abstractText
Native membranes and Triton X-100 solubilized integral membrane proteins of peroxisomes from rat liver were reconstituted in liposomes. With the patch clamp technique, a channel was detected with a conductance of 420 +/- 30 pS and a PK/PC1 of about 3. The channel in native membrane fractions was weakly voltage dependent, residing most of the time in an open state with the possibility to shift to different substates. Solubilization changed the kinetic properties. The channel became strongly voltage dependent and closed at voltages negative to -20 mV. The estimated diameter of the channel is about 1.7 nm and might explain, at least partially, the permeability properties of the peroxisomal membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
984
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Single-channel analysis of a large conductance channel in peroxisomes from rat liver.
pubmed:affiliation
Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Belgium.
pubmed:publicationType
Journal Article, In Vitro