. Author manuscript; available in PMC: 2019 Oct 22.

Published in final edited form as: Biochem Biophys Res Commun. 2019 Aug 26;518(4):651–656. doi: 10.1016/j.bbrc.2019.08.098

Table 2.

Characteristics of human chymase and CPA.

Chymase	CPA

- Single α-form of chymase is present in human MC.	- Six different isoforms of CPA (CPA-1 to CPA-6) is present in human tissues.
- Belongs to serine endopeptidase of family S1.	- Belongs to Zinc-metallocarboxypeptidase family.
- High affinity to hydrolyze Phe-His bond.	- Sequentially hydrolyzes aliphatic amino acids and aromatic amino acids from C-terminus. Low affinity for His.
- α-Chymase has high affinity for both Ang I and hAng-(1–12) substrates to directly generate Ang II.	- High affinity for hAng-(1–12)/Ang I to generate Ang-(1–9) sequentially.
- α-Chymase has low/negligible affinity to hydrolyze Ang-(1–9) into Ang II.	- Low affinity to hydrolyze Ang-(1–9) into Ang II, and subsequently Ang II into Ang-(1−7).
- Enzyme content in human adult foreskin (4.5 μg/10⁶ MC).	- Enzyme content in adult foreskin (16 μg/10⁶ MC).