Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins.

@article{Rajapakse2005BiochemicalCO,
  title={Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins.},
  author={Sanath Rajapakse and Katsueki Ogiwara and Naoharu Takano and Akihiko Moriyama and Takayuki Takahashi},
  journal={FEBS letters},
  year={2005},
  volume={579 30},
  pages={6879-84}
}
Human kallikrein 8 (KLK8) is a member of the human kallikrein gene family of serine proteases, and its protein, hK8, has recently been suggested to serve as a new ovarian cancer marker. To gain insights into the physiological role of hK8, the active recombinant enzyme was obtained in a pure state for biochemical and enzymatic characterizations. hK8 had trypsin-like activity with a strong preference for Arg over Lys in the P1 position, and its activity was inhibited by typical serine protease… CONTINUE READING
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