Linked Life Data

2546127

Source:http://linkedlifedata.com/resource/pubmed/id/2546127

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-14
pubmed:abstractText
The bradykinin receptor antagonists [D-Phe7]bradykinin, D-Arg[Hyp3,D-Phe7]bradykinin and D-Arg[Hyp3,Thi5,8,D-Phe7]bradykinin were tested for their ability to serve as substrates for kininase II (angiotensin converting enzyme) purified from rabbit lung. By HPLC, the peptides were not measurably degraded over 30 minutes. Under identical conditions, bradykinin was completely degraded to bradykinin (1-7). When hippuryl-His-Leu was used as a substrate for kininase II, the D-Phe7-substituted bradykinins acted as weak noncompetitive inhibitors. While the peptides were poor substrates for kininase II, they were short-lived when injected intravenously. D-Arg[Hyp3,D-Phe7]bradykinin was completely degraded to small fragments in less than 2 minutes. In diluted serum in vitro, a single product was observed with elution consistent with loss of arginine, suggestive of metabolism by kininase I.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-12
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:articleTitle
D-Phe7-substituted peptide bradykinin antagonists are not substrates for kininase II.
pubmed:affiliation
Nova Pharmaceutical Corporation, Baltimore, MD 21224.
pubmed:publicationType
Journal Article