The sequence A alpha-(154-159) of fibrinogen is capable of accelerating the t-PA catalysed activation of plasminogen
article
The rate of activation of plasminogen by tissue-type plasminogen activator (t-PA) is greatly increased by fibrin, but much less by fibrinogen. Fibrin(ogen) fragments such as the fibrin(ogen) cyanogen bromide fragment FCB-2 and FCB-5, and a synthetic peptide with the sequence of fibrinogen A alpha-(148-160), a constituent of FCB-2, also have rate-enhancing properties. In order to find a possibly smaller, still stimulating site within A alpha-(148-160) we synthesized successive linear amino-terminally acylated hexapeptides [i.e. A alpha-(148-153), A alpha-(149-154)'d, .... A alpha-(155-160)] from the sequence A alpha-(148-160). The only hexapeptide within the sequence A alpha-(148-160) capable of enhancing the rate of plasminogen-to-plasmin conversion by t-PA appears to be the amino-terminally acylated peptide comprising the sequence A alpha-(154-159). This peptide enhances the plasminogen activation rate six-fold; half-maximal activation rate is reached at a peptide concentration of 56 microM. Chemicals/CAS: fibrinogen, 9001-32-5; plasminogen, 9001-91-6; tissue plasminogen activator, 105913-11-9; Fibrinogen, 9001-32-5; Oligopeptides; Peptide Fragments; Plasminogen, 9001-91-6; Tissue Plasminogen Activator, EC 3.4.21.68
Topics
TNO Identifier
231541
ISSN
09575235
Source
Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis, 2(3), pp. 465-470.
Pages
465-470
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