Linked Life Data

8416802

Source:http://linkedlifedata.com/resource/pubmed/id/8416802

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-1-27
pubmed:abstractText
A new member of the endothelin/sarafotoxin family of vasoconstrictor peptides, bibrotoxin (BTX), was isolated from the venom of the burrowing asp Atractaspis bibroni by reversed-phase FPLC. The amino acid sequence of BTX differs from SRTX-b in the substitution Ala4 instead of Lys4, which suggests that it represents the peptide isoform of Atractaspis bibroni corresponding to SRTX-b. BTX competed for [125I]ET-1 binding to human ETB-type receptor with a Ki of 3.2 x 10(-9) M compared to 4.2 x 10(-9) M for SRTX-b. In rat thorax aorta BTX induced vasoconstrictions with a threshold concentration of 3 x 10(-8) M compared to 1 x 10(-9) for ET-1.
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
2
pubmed:volume
315
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
100-3
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing asp Atractaspis bibroni.
pubmed:affiliation
Research Laboratories of Schering AG, Berlin, Germany.
pubmed:publicationType
Journal Article, Comparative Study