Heat stability of carboxypeptidase R of experimental animals

Hidefumi Komura, Yasuyo Shimomura, Miho Yumoto, Hirotada Katsuya, Noriko Okada, Hidechika Okada

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Carboxypeptidase N (CPN) and carboxypeptidase R (CPR) are present in fresh serum, and cleave C-terminal arginine or lysine residues from bioactive peptides such as anaphylatoxins and kinins resulting in regulation of peptide activity. Although CPN is present in the active form in plasma, CPR is generated from proCPR by trypsin-like enzymes such as thrombin. CPR regulates not only inflammatory peptides but also restricts fibrinolysis. To elucidate the complex role of CPN and CPR in vivo, studies in animal models will be essential. CPR of guinea pig, rat and rabbit decayed at 37 C rapidly as in the case of human CPR. However, at 25 C, CPR of those species decayed to some extent, although human serum CPR did not decay within 60 min. In the presence of thrombin inhibitor, CPR in the sera of animals tested decayed more rapidly than CPR in serum without thrombin inhibitor suggesting that additional generation of CPR may have been prevented during decay evaluation. However, human serum CPR decayed more rapidly in the absence of thrombin inhibitor indicating that thrombin may accelerate the decay in human serum.

Original languageEnglish
Pages (from-to)217-223
Number of pages7
Issue number3
Publication statusPublished - 2002

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Virology


Dive into the research topics of 'Heat stability of carboxypeptidase R of experimental animals'. Together they form a unique fingerprint.

Cite this