Isolation and characterization of rabbit properdin of the alternative complement pathway.
Rabbit factor P, which is involved in stabilizing the labile C3 convertase of the alternative complement pathway, was isolated from rabbit serum by a simple two-step procedure: polyethylene glycol precipitation and QAE-Sephadex A-50 column chromatography. The chemical properties, and functional activities of the rabbit P were very similar to those of human P, except that there were slight differences in the SDS-PAGE patterns of limited tryptic digests and in the amino terminal sequences. The molecular weights were estimated to be 58 000 for rabbit P and 59 000 for human P on SDS-PAGE under reducing conditions. The amino terminal 36 residues of rabbit P showed 78% homology to the equivalent region of human P.
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D003167:Complement Activation; D050577:Complement C3-C5 Convertases / Q000378:metabolism; D003170:Complement Pathway, Alternative; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008970:Molecular Weight; D011414:Properdin / Q000302:isolation & purification* / Q000502:physiology; D011817:Rabbits / Q000097:blood* / Q000276:immunology; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D011414:Properdin; D050577:Complement C3-C5 Convertases