Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-10-14
pubmed:abstractText
Binding of 5-[3H]methylurapidil to guinea pig liver membranes was rapid, saturable, and reversible. Scatchard analysis of saturation isotherms indicated a single class of binding sites with a Kd of 0.86 nM and a Bmax of 36 fmol/mg of protein. Preincubation of the membranes with chlorethylclonidine did not alter significantly the binding parameters for 5-[3H]methylurapidil. Binding competition experiments were performed, and the order of potency for agonists was oxymetazoline > epinephrine > norepinephrine >> methoxamine; for antagonists, the potency order was (+)-niguldipine > or = 5-methylurapidil = prazosin = WB4101 > benoxathian > or = phentolamine > or = (-)-niguldipine. The binding affinity for epinephrine was modulated by the hydrolysis-resistant GTP analogue guanosine-5'-(beta, gamma-imido)triphosphate. The pharmacological profile of the 5-[3H]methylurapidil binding sites of guinea pig liver differs markedly from those of the cloned alpha 1-adrenoceptors (i.e., alpha 1B-, alpha 1C-, and alpha 1A/D-adrenoceptors) and resembles that of the classical alpha 1A receptor subtype.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
589-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Characterization of the alpha 1A-adrenoceptors of guinea pig liver membranes: studies using 5-[3H]methylurapidil.
pubmed:affiliation
Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't