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Comparative studies on human activators of plasminogen.
British Journal of Haematology
|January 1, 1981
Summary
Human activators of plasminogen, derived from plasma, endothelium, and tissue, exhibit distinct properties compared to urokinase. These novel activators are not inhibited by antiserum to urokinase, suggesting unique characteristics.
Area of Science:
- Biochemistry
- Molecular Biology
- Hematology
Background:
- Plasminogen activators are crucial for fibrinolysis.
- Urokinase is a well-characterized urinary plasminogen activator.
- The existence and properties of endogenous tissue and plasma activators are of significant interest.
Purpose of the Study:
- To isolate and characterize human plasminogen activators from various endogenous sources.
- To compare the properties of these activators with urokinase.
- To investigate the immunological relationship between endogenous activators and urokinase.
Main Methods:
- Preparation of plasminogen activators from human plasma, blood vessel endothelium, and tissue.
- Biochemical and functional characterization of the purified activators.
- Immunological assays using antiserum against urokinase.
Main Results:
- Activators were successfully prepared from plasma, endothelium, and tissue.
- These endogenous activators displayed physical and functional properties distinct from urokinase.
- Antiserum to urokinase neutralized urokinase activity but did not affect the activity of the plasma, endothelial, or tissue activators.
Conclusions:
- Human plasma, endothelial, and tissue contain distinct plasminogen activators.
- These endogenous activators differ significantly from urokinase.
- The findings suggest that endogenous plasminogen activators represent a separate class of molecules from urokinase, with potential implications for understanding fibrinolysis and developing new therapeutic agents.