Dysfunctional plasminogen in full term newborn--study of active site of plasmin.
The functional activity and active site of plasmin in full-term newborns have been studied and compared to those in adults in order to investigate the nature of the abnormality found in newborn plasminogen described in a previous paper. The functional activity of newborn plasminogen measured on chromogenic substrate was approximately 18% that of adult plasminogen when streptokinase was used as an activator and 12% when urokinase was used. Proteolysis of newborn plasminogen by urokinase yielding a two-chain plasmin form occurred normally, but the incorporation of diisopropylphosphorofluoridate into the light chain of newborn plasmin was approximately 23% of that observed in the light chain of adult plasmin. These observations suggest that the abnormality of full-term newborn plasminogen is located in the active site of the molecule.
D000328:Adult; D001665:Binding Sites; D005260:Female; D005312:Fetal Blood / Q000032:analysis; D005341:Fibrinolysin / Q000032:analysis*; D006801:Humans; D007231:Infant, Newborn; D007531:Isoflurophate / Q000378:metabolism; D008297:Male; D010958:Plasminogen / Q000032:analysis*; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism
D007531:Isoflurophate; D010958:Plasminogen; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator