Isolation of an iC3b forming enzyme from peritoneal polymorphonuclear leukocytes of guinea pigs

Abstract

We have investigated fluid phase cleavage of C3b by peritoneal polymorphonuclear leukocytes of guinea pigs and found that polymorphonuclear leukocytes expressed an iC3b forming enzyme as well as C3b receptor with maturation in peritoneal cavity. The iC3b forming enzyme was found to be distinct from C3bINA, a physiological iC3b forming enzyme in plasma, since the activity was inhibited by monoiodoacetic acid and did not require a cofactor plasma protein, β1H, for the cleavage of C3b into iC3b. The iC3b forming enzyme is gradually released upon incubation of PMN at 37°C. The molecular weight of the iC3b forming enzyme was estimated to be 48,000 from gel filtration on Sephadex G-200.