Linked Life Data

1466270

Source:http://linkedlifedata.com/resource/pubmed/id/1466270

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-1-15
pubmed:abstractText
Besides guanidino compounds and amines structurally related to arginine and lysine, compounds with other cationic groups are inhibitors of trypsin-like serine proteinases. Particularly aromatic ring structures with an amidino moiety have high affinity for these enzymes. In most cases ordinary benzamidine derivatives are no selective inhibitors, however, among derivatives of N alpha-arylsulfonyl-omega-amidinophenyl-alpha-amino-alkylcarboxylic acids selective competitive inhibitors of several enzymes were found. Amides of phenyl-alpha-aminobutyric acid containing an amidino moiety are inhibitors of plasma kallikrein. The p-amidinoanilide of 2-tosylamino-4-phenylbutyric acid inhibits selectively plasma kallikrein with a Ki of 0.70 mumol/l. In contrast, potent and selective inhibitors of glandular kallikrein were hardly found among benzamidines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0379-0363
pubmed:author
pubmed:issnType
Print
pubmed:volume
38 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
190-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Inhibition of glandular and plasma kallikrein by benzamidine derivatives.
pubmed:affiliation
Institute of Pharmacology & Toxicology, Medical Academy Erfurt, FRG.
pubmed:publicationType
Journal Article, In Vitro