Pseudomonas aeruginosa elastase was found to be a typical metallo-neutral proteinase. 1) The enzyme behaved with the same pattern in affinity chromatography with Sepharose-ε-aminocaproyl-D-phenylalanine methyl ester as the other neutral proteinases. 2) It contained 0.9 atom Zn per molecule. 3) It showed its specificity against aromatic or hydrophobic amino acid residues at the amino-side of the splitting point.
