Linked Life Data

1718428

Source:http://linkedlifedata.com/resource/pubmed/id/1718428

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
1991-12-20
pubmed:abstractText
Monoiodotyrosine ([125I]ChTX) binds with high affinity to a single class of receptors present in bovine aortic smooth muscle sarcolemmal membranes that are functionally associated with the high-conductance Ca(2+)-activated K+ channel [maxi-K channel; Vázquez, J., et al. (1989) J. Biol. Chem. 265, 20902-20909]. Cross-linking experiments carried out with this preparation in the presence of [125I]ChTX and disuccinimidyl suberate indicate specific incorporation of radioactivity into a protein of Mr 35,000. The smooth muscle ChTX receptor can be solubilized in active form in the presence of selected detergents. Treatment of membranes with digitonin releases about 50% of the ChTX binding sites. The solubilized receptor retains the same biochemical and pharmacological properties that are characteristic of toxin interaction with membrane-bound receptors. The solubilized receptor binds specifically to wheat germ agglutinin-Sepharose resin, suggesting that it is a glycoprotein. Functional ChTX binding sites can also be solubilized in 3-[(3-cholamidopropyl)dimethylamino]-1-propanesulfonate (CHAPS). Sucrose density gradient centrifugation of either digitonin or CHAPS extracts indicates that the ChTX receptor has a high apparent sedimentation coefficient (s20,w = 23 and 18 S, respectively). Cross-linking experiments indicate that the appearance of the 35-kDa membrane protein correlates with ChTX binding activity after both wheat germ agglutinin-Sepharose and sucrose density gradient centrifugation steps. Given the high apparent sedimentation coefficient of the ChTX receptor, the 35-kDa membrane protein may be a subunit of a higher molecular weight complex which forms the maxi-K channel in smooth muscle sarcolemma.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11157-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Characterization of the solubilized charybdotoxin receptor from bovine aortic smooth muscle.
pubmed:affiliation
Department of Membrane Biochemistry and Biophysics, Merck Institute for Therapeutic Research, Rahway, New Jersey 07065.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.