The extrusion of protein from the rabbit polymorphonuclear leucocyte treated with staphylococcal leucocidin

Abstract

The effect of leucocidin on the distribution of protein and nucleic acid in subcellular fractions of the leukocyte has been assessed. Ribonuclease, deoxyribo-nuclease, [beta]-glucuronidase and peroxidase have been found to be present in the proteins liberated from the leukocyte by leucocidin. It is concluded that the protein released by leucocidin from the leukocyte is derived mainly if not entirely from the cell granules. There is an increased incorporation of P32 into the phospholipids of the leukocyte, which is largely localized in an acidic lipid distinct from phosphoinosi-tide. There is no increased incorporation of p32 into the ribonucleic acids of the leukocyte during leucocidin action.