Abstract
Publisher Summary This chapter describes the simpler, higher yield method for purifying factor D from urine of patients with tubular dysfunction and from peritoneal dialysis fluid. The chapter also discusses the recent information on the structure and properties of factor D. Complement factor D is an essential component of the alternative pathway of complement activation. It is a serine proteinase with low catalytic activity against synthetic substrates 2 and a single known natural substrate, complement factor B. Several hemolytic assays are available for measuring factor D activity. This assay involves the use of rabbit erythrocytes and of a serum reagent depleted of factor D (RD). The amino acid sequence of factor D shows a high degree of homology to that of other serine proteinases, exhibiting 33–35% amino acid residue identity with pancreatic bovine trypsin, bovine chymotrypsin A, porcine elastase, and human neutrophil elastase. In addition to RD procedures, a number of more quantitative assays using cellular intermediates and purified complement components are also described in the chapter.
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