Characterization of a recombinant granzyme B derivative as a "restriction" protease.

Abstract

Blood coagulation factor Xa (FXa) and Thrombin are well-known serine proteases often used for processing of recombinant fusion proteins, but because they are purified from bovine blood or other animal sources, there is a risk of pathogenic contaminants in the preparation of the proteases. We report here the characterization of a recombinant serine protease produced in Escherichia coli, which can be used as a specific and efficient alternative to FXa and Thrombin as processing protease. This recombinant protease is derived from human granzyme B (GrB). The protease is found to be very stable in general, and it performs very well in the cleavage of several different fusion proteins tested and was even found superior to processing by FXa in two cases.

Cite this paper

@article{Fynbo2005CharacterizationOA, title={Characterization of a recombinant granzyme B derivative as a "restriction" protease.}, author={Charlotte Harkjaer Fynbo and Rikke H\oegh Lorentsen and Michael Etzerodt and Hans Christian Th\ogersen and Thor Las Holtet}, journal={Protein expression and purification}, year={2005}, volume={39 2}, pages={209-18} }