Linked Life Data

1662495

Source:http://linkedlifedata.com/resource/pubmed/id/1662495

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-2-7
pubmed:abstractText
Optimal conditions for biotinylation of endothelin-1 (Et-1) were determined using biotinylating reagents of variable linker arm length and mono- vs dual-biotinylated Et-1. Specific modification of lysine-9 sidechain with NHS-LC-biotin (Et-1[BtK9]) produced a derivative with maximal binding and retention of vascular smooth muscle contractile activity. The Et-1[BtK9] probe bound to Chinese hamster ovary cells transfected with EtA receptor cDNA (CHO[EtR]), but not untransfected cells. Binding to rat vascular smooth muscle cells (VSMC) was detectable at 0.01 nM with maximal binding at 1 nM. Displacement of 1 nM Et-1 [BtK9] binding by Et-1 indicated an IC50 value of 6 +/- 3 nM. Et-1 displaced Et-1[BtK9] binding to VSMC and CHO[EtR] to a greater extent than endothelin-3, indicating predominant expression of EtA receptor sub-type. Thus, biotinylation of Et-1 at the lysine-9 sidechain may be of general use for localization and typing of Et-receptor populations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1245-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Evaluation of endothelin receptor populations using endothelin-1 biotinylated at lysine-9 sidechain.
pubmed:affiliation
Department of Biochemistry & Molecular Biology, Albany Medical College, NY 12208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't