Abstract
Several cationic proteins of human granulocytes possess chymotrypsin-like and bactericidal activities. The heat-labile chymotrypsin-like activity is inhibited by serum, owing to complex formation wiui α2-macroglobulin and α1-antitrypsin. The molar affinity of the cationic proteins for α2-macroglobu-lin is much higher than that for α1-antitrypsin. The results indicate that the molar combining ratios are 1:1 for cationic protein to α1-antitrypsin and 2:1 for cationic protein to α2-macroglobulin. The proteolytic activity against fibrinogen and casein is inhibited by both α2-macroglobulin and α1-antitrypsin, whereas the activity against small molecular synthetic substrates is inhibited by α1-antitrypsin but not α2-macroglobulin. The heat-stable bactericidal action of the cationic proteins against Staphylococcus was also inhibited by serum, probably owing to complex formation with α2-macroglobulin and α1-antitrypsin.