Isolation and partial characterization of bovine and equine factor D.
Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5-17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, respectively. Functionally, both equine and bovine D would reconstitute a human reagent deficient in D (RD), while human or equine D would substitute for bovine D when using a bovine RD. Neither bovine, equine or human D would, however, reconstitute an equine RD.
D000818:Animals; D002417:Cattle / Q000276:immunology*; D002845:Chromatography; D003166:Complement Activating Enzymes / Q000302:isolation & purification*; D011416:Complement Factor D / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen; D006461:Hemolysis; D006736:Horses / Q000276:immunology*; D008970:Molecular Weight
D005340:Fibrinogen; D003166:Complement Activating Enzymes; C493488:CFD protein, human; D011416:Complement Factor D