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Activation of proPHBSP, the Zymogen of a Plasma Hyaluronan Binding Serine Protease, by an Intermolecular Autocatalytic Mechanism by Michael Etscheid; Andreas Hunfeld; Herbert König; Rainer Seitz; Johannes Dodt is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The hyaluronic acid binding serine protease (PHBSP), an enzyme with the ability to activate the coagulation factor FVII and the plasminogen activator precursors and to inactivate factor VIII and factor V, could be isolated from human plasma in the presence of 6 M urea as a single-chain zymogen, whereas under native conditions only its activated two-chain form was obtained. The total yield of proenzyme (proPHBSP) was 5 -6 mg/l, corresponding to a concentration of at least 80 -100 nM in plasma. Upon removal of urea, even in the absence of charged surfaces a rapid development of amidolytic activity was observed that correlated with the appearance of the two-chain enzyme. The highest activation rate was observed at pH 6. ProPHBSP processing was concentration-dependent following a second order kinetic and was accelerated by catalytic amounts of active PHBSP, indicating an intermolecular autocatalytic activation. Charged macromolecules like poly-L-lysine, heparin, and dextran sulfate strongly accelerated the autoactivation, suggesting that in vivo proPHBSP activation might be a surface-bound process. The intrinsic activity of the proenzyme was determined to be 0.25 -0.3%, most likely due

Who reads Activation of proPHBSP, the Zymogen of a Plasma Hyaluronan Binding Serine Protease, by an Intermolecular Autocatalytic Mechanism?

Author

Michael Etscheid; Andreas Hunfeld; Herbert König; Rainer Seitz; Johannes Dodt

Publisher

Walter de Gruyter GmbH

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)