Heat stability of carboxypeptidase R of experimental animals

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

研究成果: Article査読

11 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)217-223
ページ数7
ジャーナルMICROBIOLOGY and IMMUNOLOGY
46
3
DOI
出版ステータスPublished - 01-01-2002
外部発表はい

All Science Journal Classification (ASJC) codes

  • 微生物学
  • 免疫学
  • ウイルス学

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