The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.

@article{Lin2001TheHC,
  title={The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.},
  author={Lin Lin and Istvan Sohar and Henry Lackland and Peter Lobel},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 3},
  pages={2249-55}
}
The CLN2 gene mutated in the fatal hereditary neurodegenerative disease late infantile neuronal ceroid lipofuscinosis encodes a lysosomal protease with tripeptidyl-peptidase I activity. To understand the enzymological properties of the protein, we purified and characterized C-terminal hexahistidine-tagged human CLN2p/tripeptidyl-peptidase I produced from insect cells transfected with a baculovirus vector. The N terminus of the secreted 66-kDa protein corresponds to residue 20 of the primary… CONTINUE READING
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