Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.

@article{Campbell2002InactivationOC,
  title={Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.},
  author={William D Campbell and Eliada Lazoura and Noriko Okada and Hidechika Okada},
  journal={Microbiology and immunology},
  year={2002},
  volume={46 2},
  pages={131-4}
}
Pro-carboxypeptidase R (proCPR), also known as thrombin-activatable fibrinolysis inhibitor (TAFI), precursor of carboxypeptidase U and plasma carboxypeptidase B is present in plasma and following activation by thrombin/thrombomodulin and/or plasmin can remove arginine from the carboxyterminal of C3a and C5a. We have shown that this enzyme can remove terminal arginine from the C5a octapeptide much more efficiently than the classical anaphylatoxin inactivator, carboxypeptidase N (CPN). Since we… CONTINUE READING

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