Inactivation of human lung tryptase: evidence for a re-activatable tetrameric intermediate and active monomers.

@article{Addington1996InactivationOH,
  title={Inactivation of human lung tryptase: evidence for a re-activatable tetrameric intermediate and active monomers.},
  author={A K Addington and David S. Johnson},
  journal={Biochemistry},
  year={1996},
  volume={35 42},
  pages={13511-8}
}
Human lung tryptase (HLT), a trypsin-like serine proteinase stored as an active enzyme in association with heparin in mast cell granules, is released into the extracellular environment when mast cells are activated. Tryptases are unusual in that they form tetramers and bind heparin. As there are no known endogenous tryptase inhibitors, loss of heparin and dissociation of the active tetrameric enzyme to inactive monomers has been proposed as the mechanism of control. Activity and intrinsic… CONTINUE READING

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