A novel chymotrypsin-like serine proteinase from human lung.

A novel chymotrypsin-like serine proteinase with an M(r) of 30,000 has been isolated from human lung tissue. The enzyme was active on both the synthetic substrate Suc-Ala-Ala-Pro-Phe-SBzl and azocasein, with a pH optimum of 8.0 and a preference for high concentrations of NaCl for maximum activity. The proteinase was inhibited by diisopropylfluorophosphate, tosyl-phenylalanyl-chloromethane, chymostatin, soybean trypsin inhibitor, alpha-1-antichymotrypsin, and alpha-2-macroglobulin. It was not inhibited by C-1 inhibitor or aprotinin. An N-terminal sequence of IIGGTESKPDSRPYMALLQIVEPAVH indicated that this enzyme is a member of a superfamily of serine proteinases comprising cathepsin G, chymase, and the granzymes; however, it is clearly distinct from these enzymes on the basis of both physical and chemical properties.