Linked Life Data

8165620

Source:http://linkedlifedata.com/resource/pubmed/id/8165620

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-5-23
pubmed:abstractText
Tissue factor (TF) markedly enhances the ability of factor VIIa (FVIIa) to cleave both macromolecular and small peptidyl substrates. Using soluble mutant TF (sTF) to investigate TF-enhanced FVIIa amidolytic activity in solution, we screened thirty-four commercially available peptidyl-p-nitroanilide substrates and found that substrate hydrolysis rates were influenced by both the peptide sequence and the N-terminal blocking group (MeSO2 > MeO-CO or free N-terminus >> benzoyl). Two substrates (Chromozym t-PA: MeSO2-D-Phe-Gly-Arg-pNA; and CBS 34.47: H-D-cyclohexylglycyl-alpha-aminobutyryl-Arg-pNA) were cleaved at rates higher than those of previously reported chromogenic substrates for FVIIa. The pH range of FVIIa amidolytic activity toward Chromozym t-PA was 6.5 to 10 with an optimum at pH 7.8, while sTF.VIIa had a higher pH optimum (pH 8.4 to 8.5). The degree of enhancement of FVIIa activity by sTF varied from 12-fold at pH 7.5 to 73-fold at pH 9.9. The effect of a variety of agents on FVIIa amidolytic activity was surveyed: most decreased activity, while glycerol and ethylene glycol enhanced the activity of FVIIa but not sTF.VIIa. These results indicate that the effect of sTF on the catalytic center of FVIIa is pH-dependent, and that certain polyalcohols can partially substitute for TF.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
970-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Importance of substrate composition, pH and other variables on tissue factor enhancement of factor VIIa activity.
pubmed:affiliation
Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't