Abstract
Mouse peritoneal macrophages synthesized and secreted a precursor (pro-C5) of the fifth component of serum complement (C5) in short-term tissue culture. Approximately 0.2% of the newly synthesized intracellular protein and 0.8% of secreted protein were precipitable with antiserum to mouse C5. The precursor is similar in size to the native serum protein (210,000 daltons), but consists of a single polypeptide chain. In contrast, serum C5 consists of two polypeptide chains (m.w. 125,000 and 83,000) linked by disulfide bridges. An electrophoretic variant of pro-C5 distinct from intracellular C5 was detected in medium from macrophage cultures.