Recombinant expression, purification, and kinetic and inhibitor characterisation of human site-1-protease.

@article{Bodvard2007RecombinantEP,
  title={Recombinant expression, purification, and kinetic and inhibitor characterisation of human site-1-protease.},
  author={Kristofer Bodvard and Johanna Mohlin and Wolfgang G. Knecht},
  journal={Protein expression and purification},
  year={2007},
  volume={51 2},
  pages={308-19}
}
Human site-1-protease (S1P, MEROPS S08.8063), also widely known as subtilisin/kexin isozyme 1 (SKI-1), is a membrane bound subtilisin-related serine protease, that belongs to a group of nine mammalian proprotein convertases. Among these proteases, S1P displays unique substrate specificity, by showing preferred cleavage after non-basic amino acids. S1P plays a key role in a proteolytic pathway that controls the cholesterol content of membranes, cells and blood. S1P also participates in the… CONTINUE READING

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