Chymase is a kind of serine proteinase, mainly exists in secretory granules of mast cell and extracellular interstitium. The mature enzyme is a glycoprotein comprising 226 amino acid residues, with molecular weight of 30 kD. It can be inhibited by serine proteinase inhibitors but not by angiotensin I converting enzyme inhibitors. The cDNA and genomic DNA of human chymase were cloned and sequenced. Chymase has close relations with neurogenic inflammation, extracellular matrix catabolism, control of vasoactive peptide metabolism, and so on. It plays an important role in angiotensin II formation in human heart.