Linked Life Data

2002458

Source:http://linkedlifedata.com/resource/pubmed/id/2002458

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-4-17
pubmed:abstractText
C-Terminal fragment analogues of the leech protein hirudin or the related protein hirudin PA block thrombin's cleavage of fibrinogen. Three series of synthetic peptides were synthesized to study the effects of sulfation in hirudin-derived peptides. Potency of hirudin analogues increased with p-(amino)Phe63, p-(aminosulfonate)Phe63, and p-(sulfate)Tyr63 substitution in place of Tyr63. Sulfation of Tyr56, which in hirudin is normally Phe, resulted in a loss of 1 order of magnitude in potency. The sulfation of Tyr64 of the hirudin PA related analogue resulted in increased potency as for the hirudin analogue. However, in this series the p-(amino)Phe64 and p-(amino-sulfonate)Phe64 did not have increased potency. In addition to these positional effects, replacing all the Glu residues with (O-sulfato)Ser yielded an analogue with full antithrombin potency.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1184-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Positional effects of sulfation in hirudin and hirudin PA related anticoagulant peptides.
pubmed:affiliation
Merrel Dow Research Institute, Cincinnati, Ohio 45215.
pubmed:publicationType
Journal Article, Comparative Study