Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen.

@article{Molloy1992HumanFI,
  title={Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen.},
  author={Sean S. Molloy and Patricia A. Bresnahan and Stephen H Leppla and Kurt R. Klimpel and Gary Thomas},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 23},
  pages={
          16396-402
        }
}
Previous work demonstrated that human furin is a predominantly Golgi membrane-localized endoprotease that can efficiently process precursor proteins at paired basic residues (-Lys-Arg- or -Arg-Arg-) in transfected cells. Anion-exchange chromatography of culture supernatant from cells expressing a soluble truncated form of human furin resulted in a greatly enriched preparation of the endoprotease (approximately 70% pure as determined by protein staining). Enzymatic studies show that furin is a… CONTINUE READING
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