Identification of P-57, a serine proteinase, from human erythrocyte membranes, which cleaves both chains of human third component (C3) of complement.
A proteinase, which cleaves human third component of complement, was solubilized from erythrocyte membranes then purified by gel filtration chromatography, fluid phase electrophoresis, and hydroxylapatite chromatography. Labeling of the purified material by 125I or 3H-DFP and measurement of proteolytic activity subsequently isolated by SDS-polyacrylamide gel electrophoresis allowed to identify a 57 kDa single band, in non reducing conditions. Inhibition of this activity by PMSF supports covalent modification of an active serine residue. This membrane serine proteinase cleaved alpha and beta chains of human third component of complement, suggesting that p-57 is distinct from plasma serine proteinases.
D002499:Centrifugation, Density Gradient; D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel; D003176:Complement C3 / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000097:blood* / Q000302:isolation & purification; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D006868:Hydrolysis; D012697:Serine Endopeptidases
D003176:Complement C3; D010450:Endopeptidases; D012697:Serine Endopeptidases; C050640:serine proteinase P-57