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Surface adsorption and fibrinogen interactions with hirudin-thrombin complex
1Center for Controlled Chemical Delivery, University of Utah, Salt Lake City 84112, USA.
This study describes the protein interaction properties of hirudin-thrombin complex adsorbed onto a surface. Hirudin-thrombin complex, preadsorbed thrombin bound with hirudin, and thrombin were coated onto the surfaces of glass beads. The activity of the thrombin component adsorbed onto the surface, and hence the ability of hirudin to bind and inactivate thrombin, was determined by measuring the activity of thrombin to cleave fibrinogen to generate fibrin and to cleave a chromogenic substrate, S-2238. Pure thrombin adsorbed on the surface (without hirudin) retained its activity to cleave fibrinogen and cleave S-2238. Hirudin-thrombin complex adsorbed on the surface did not stimulate the activation of fibrinogen, nor did it cleave S-2238.
This study describes the protein interaction properties of hirudin-thrombin complex adsorbed onto a surface. Hirudin-thrombin complex, preadsorbed thrombin bound with hirudin, and thrombin were coated onto the surfaces of glass beads. The activity of the thrombin component adsorbed onto the surface, and hence the ability of hirudin to bind and inactivate thrombin, was determined by measuring the activity of thrombin to cleave fibrinogen to generate fibrin and to cleave a chromogenic substrate, S-2238. Pure thrombin adsorbed on the surface (without hirudin) retained its activity to cleave fibrinogen and cleave S-2238. Hirudin-thrombin complex adsorbed on the surface did not stimulate the activation of fibrinogen, nor did it cleave S-2238.