Linked Life Data

2436306

Source:http://linkedlifedata.com/resource/pubmed/id/2436306

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1987-5-4
pubmed:abstractText
Sodium channel proteins have now been isolated from a number of nerve and muscle preparations. All are characterized by the presence of a very large glycoprotein subunit of approximately 260 kilodaltons which may contain the structural features required for voltage-dependent channel gating and cation selectivity. These purified proteins have been reconstituted into vesicle systems and planar bilayers and demonstrate the ensemble and single-channel behavior characteristic of the native sodium channel. Although the sodium channel from eel appears to consist of only the 260-kilodalton protein, the channels from rat brain and rat or rabbit skeletal muscle contain one or more smaller subunits of 37-39 kilodaltons. In skeletal muscle, a 38-kilodalton subunit is present in both conventionally purified channel and channel isolated with immunoaffinity techniques. The stoichiometry of the large (alpha) and the small (beta) subunits appears to be 1:1 in skeletal muscle but 1:2 in rat brain. The role of the small subunits in the normal functioning of the sodium channel remains to be defined.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0094-7733
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-48
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Voltage-sensitive sodium channels: an evolving molecular view.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't