H-D-val-leu-lys-aminoisophthalic acid, dimethyl ester, is sensitive to streptokinase-activator not to plasmin.
Am J Clin Pathol
; 75(3): 372-7, 1981 Mar.
Article
en En
| MEDLINE
| ID: mdl-6452054
ABSTRACT
The ability of human plasma and purified human plasmin and plasminogen to hydrolyze a new synthetic substrate, H-D-valine-leucine-lysine-5-aminoisophthalic acid, dimethyl ester, ditrifluoroacetate, was studied. Contrary to published data, we found this substrate was only minimally hydrolyzed by plasmin or urokinase-treated plasminogen or plasma. Plasminogen-free bovine fibrinogen was readily degraded by plasmin and urokinase-activated plasminogen. However, in the presence of streptokinase, the synthetic substrate was highly sensitive to human plasma and purified plasmin and plasminogen. Apparently, the substrate is specific for streptokinase-plasmin and streptokinase-plasminogen activators, not for plasmin.
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Banco de datos:
MEDLINE
Asunto principal:
Ácidos Ftálicos
/
Estreptoquinasa
/
Fibrinolisina
/
Colorantes Fluorescentes
Tipo de estudio:
Diagnostic_studies
Límite:
Humans
Idioma:
En
Año:
1981
Tipo del documento:
Article