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- W2040551353 abstract "Comparison of the primary structures of high-Mr urokinase and tissue-type plasminogen activator reveals a high degree of structural homology between the two proteins, except that tissue activator contains a 43 residue long amino-terminal region, which has no counterpart in urokinase. We show that this segment is homologous with the finger-domains responsible for the fibrin-affinity of fibronectin. Limited proteolysis of the amino-terminal region of plasminogen activator was found to lead to a loss of the fibrin-affinity of the enzyme. It is suggested that the finger-domains of fibronectin and tissue-types plasminogen activator have similar functions and that the finger-domains of the two proteins evolved from a common ancestral fibrin-binding domain." @default.
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- W2040551353 date "1983-10-31" @default.
- W2040551353 modified "2023-09-30" @default.
- W2040551353 title "Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator" @default.
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- W2040551353 doi "https://doi.org/10.1016/0014-5793(83)81157-0" @default.
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