[Proteolytic activity of the Glu-plasminogen complex with fibrinogen fragment E].
Glu-plasminogen interaction with fibrinogen fragment E results in the alteration of its adsorptive capacity. During this interaction in the absence of plasmin and tissue activator of plasminogen, Glu-plasminogen is transformed into a partly degraded form. Glu-plasminogen complexes with soluble and immobilized fibrinogen fragment E. contain a serine proteinase-specific activity which is inhibited by diisopropylfluorophosphate. The complexes under study are active towards fibrin and the plasmin-specific tripeptide substrate, D-Val-L-Leu-L-Lys-p-nitroanilide. It is concluded that fibrinogen fragment E induces structural changes in the enzyme molecule which eventually result in the formation of an active center.
Skomorovskaia
E V
EV
Grinenko
T V
TV
Kudinov
S A
SA
Zolotareva
E N
EN
D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D005342:Fibrinolysis; D006801:Humans; D006868:Hydrolysis; D010958:Plasminogen / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism
D005338:Fibrin Fibrinogen Degradation Products; C018543:fibrinogen fragment E; D010958:Plasminogen; D012697:Serine Endopeptidases
Issledovanie proteolitcheskoĭ aktivnosti kompleksa Glu-plasminogena s fragmentom E fibrinogena.