Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1985-1-22
|
pubmed:abstractText |
A series of C-terminal peptide segments of gastrin, i.e., (tert-butyloxycarbonyl)-L-tryptophyl-L-methionyl-L-aspartic acid amide, (tert-butyloxycarbonyl)-glycyl-L-tryptophyl-L-methionyl-L-aspartic acid amide, (tert-butyloxy-carbonyl)-L-tyrosyl-glycyl-L-tryptophyl-L-methionyl-L-asp artic acid amide, and (benzyloxycarbonyl)-L-glutamyl-L-alanyl-L-tyrosyl-glycyl-L-tryptophyl-L -methionyl-L-aspartic acid amide were prepared and were shown to competitively inhibit the binding of labeled human gastrin to its receptors in an isolated gastric mucosal cell preparation and to antagonize the action of gastrin on gastric acid secretion (ED50 from 1.5 to 7 mg/kg) in vivo in the reperfused rat stomach, determined according to the method of Ghosh and Schild. From these studies, it could be concluded that the C-terminal phenylalanine residue, which is of primary importance for intrinsic biological gastrin-like activity, is not essential for binding to gastrin receptors.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0022-2623
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
27
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1597-601
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:6094810-Amino Acid Sequence,
pubmed-meshheading:6094810-Animals,
pubmed-meshheading:6094810-Drug Evaluation, Preclinical,
pubmed-meshheading:6094810-Gastric Mucosa,
pubmed-meshheading:6094810-Gastrins,
pubmed-meshheading:6094810-Peptide Fragments,
pubmed-meshheading:6094810-Rats,
pubmed-meshheading:6094810-Receptors, Cell Surface,
pubmed-meshheading:6094810-Receptors, Cholecystokinin,
pubmed-meshheading:6094810-Structure-Activity Relationship
|
pubmed:year |
1984
|
pubmed:articleTitle |
Synthesis and biological activity of new peptide segments of gastrin exhibiting gastrin antagonist property.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|