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• W2078304957 endingPage "2182" @default.
• W2078304957 startingPage "2176" @default.
• W2078304957 abstract "A variant of recombinant plasminogen with the plasmin active site serine (S741) replaced by cysteine was produced and labeled with fluorescein at this residue to provide the derivative Plg(S741C-fluorescein). Studies of cleavage, conformation, and fibrin-binding properties of the derivative showed it to be a good model substrate to study plasminogen activation. Both in solution and in a fully polymerized fibrin clot, cleavage of the single chain zymogen to the two-chain “plasmin” molecule was accompanied by a 50% quench of fluorescence intensity. This change allows facile, continuous monitoring of the kinetics of cleavage. Measurements of cleavage by single chain t-PA within intact, fully polymerized 3 μM fibrin yielded apparent kcat and Km values of (0.08 s-1, 0.52 μM) and (0.092 s-1, 0.098 μM) for [Glu1]- and [Lys78]Plg(S741C-fluorescein), respectively. These values are similar to those obtained by others with plasma plasminogen. The approach used here might generally be useful in simplifying the analysis of zymogen activation kinetics in cases where the product (protease) has a great influence on its own formation via positive or negative feedback loops. A variant of recombinant plasminogen with the plasmin active site serine (S741) replaced by cysteine was produced and labeled with fluorescein at this residue to provide the derivative Plg(S741C-fluorescein). Studies of cleavage, conformation, and fibrin-binding properties of the derivative showed it to be a good model substrate to study plasminogen activation. Both in solution and in a fully polymerized fibrin clot, cleavage of the single chain zymogen to the two-chain “plasmin” molecule was accompanied by a 50% quench of fluorescence intensity. This change allows facile, continuous monitoring of the kinetics of cleavage. Measurements of cleavage by single chain t-PA within intact, fully polymerized 3 μM fibrin yielded apparent kcat and Km values of (0.08 s-1, 0.52 μM) and (0.092 s-1, 0.098 μM) for [Glu1]- and [Lys78]Plg(S741C-fluorescein), respectively. These values are similar to those obtained by others with plasma plasminogen. The approach used here might generally be useful in simplifying the analysis of zymogen activation kinetics in cases where the product (protease) has a great influence on its own formation via positive or negative feedback loops." @default.
• W2078304957 created "2016-06-24" @default.
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• W2078304957 date "1997-01-01" @default.
• W2078304957 modified "2023-10-18" @default.
• W2078304957 title "Production and Characterization of Recombinant Human Plasminogen(S741C-Fluorescein)" @default.
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• W2078304957 doi "https://doi.org/10.1074/jbc.272.4.2176" @default.
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