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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-5-12
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pubmed:abstractText |
Scatchard-plot analysis of [125I]ET-1 and [125I]ET-3 binding to rat lung membranes exhibited almost the same Kd values whereas the concentration of the binding sites of ET-1 is approximately four times higher than that of ET-3. This result suggests the presence of at least two distinct subtypes of ET receptors: an ET-1-specific type and an ET-3-specific or ET-1 and ET-3 nonselective type. On the other hand, in rat brain membranes, a curvilinear Scatchard plot was obtained for [125I]ET-3 in contrast to a linear plot for [125I]ET-1. This finding also demonstrates the existence of the two different receptor subtypes having the same affinity for ET-1, but one of which has a high affinity and the other has a low affinity for ET-3. Moreover, these data indicate that an ET receptor subtype exists in rat brain different from the subtype in rat lung. To obtain the bases for a further detailed characterization of the receptor, we have purified the rat lung ET receptor to homogeneity by ET-1-affinity chromatography. The purified receptor exhibits a molecular mass of 45 kDa, in good agreement with that estimated from the affinity labeling.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0160-2446
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17 Suppl 7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S122-3
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1725304-Animals,
pubmed-meshheading:1725304-Brain Chemistry,
pubmed-meshheading:1725304-Endothelins,
pubmed-meshheading:1725304-Kinetics,
pubmed-meshheading:1725304-Lung,
pubmed-meshheading:1725304-Male,
pubmed-meshheading:1725304-Membranes,
pubmed-meshheading:1725304-Rats,
pubmed-meshheading:1725304-Rats, Inbred Strains,
pubmed-meshheading:1725304-Receptors, Cell Surface,
pubmed-meshheading:1725304-Receptors, Endothelin
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pubmed:year |
1991
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pubmed:articleTitle |
Characterization of endothelin receptor subtypes.
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pubmed:affiliation |
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro
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