rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1996-2-27
|
pubmed:abstractText |
The coexpression of the rat Kv beta 1 subunit with the mouse Kv1.1 (mKv1.1) K+ channel in Chinese hamster ovary cells caused an increase in the rate of inactivation of whole-cell current. Current decayed in a bi-exponential fashion with a fast voltage-dependent and a slower voltage-independent component. The inactivating current component accounted for around 40% of the total outward current. In contrast to previous studies using K+ channel alpha subunits, peptides based on the N-terminal of the Kv beta 1 subunit were unable to mimic the action of the entire subunit. The findings indicate differences between the inactivation induced by the Kv beta 1 subunit and the N-type inactivation mechanism associated with certain rapidly-inactivating cloned K+ channel alpha subunits.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
378
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
250-2
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8557111-Amino Acid Sequence,
pubmed-meshheading:8557111-Animals,
pubmed-meshheading:8557111-CHO Cells,
pubmed-meshheading:8557111-Cricetinae,
pubmed-meshheading:8557111-Electrophysiology,
pubmed-meshheading:8557111-Kv1.1 Potassium Channel,
pubmed-meshheading:8557111-Molecular Sequence Data,
pubmed-meshheading:8557111-Patch-Clamp Techniques,
pubmed-meshheading:8557111-Peptide Fragments,
pubmed-meshheading:8557111-Potassium Channels,
pubmed-meshheading:8557111-Potassium Channels, Voltage-Gated,
pubmed-meshheading:8557111-Recombinant Proteins,
pubmed-meshheading:8557111-Transfection
|
pubmed:year |
1996
|
pubmed:articleTitle |
The modulation of the rate of inactivation of the mKv1.1 K+ channel by the beta subunit, Kv beta 1 and lack of effect of a Kv beta 1 N-terminal peptide.
|
pubmed:affiliation |
Electrophysiology Laboratory, Wyeth Research-UK, Taplow, Berkshire, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|