The hemolytic equivalence of human, guinea pig and canine complement proteins.
The ability of functionally pure human, guinea pig and canine complement proteins to fulfill the hemolytic function of a substituted analagous component in an otherwise totally homogeneous complement sequence was investigated by means of conventional hemolytic assays. A striking feature was the observation that for hemolysis to occur, differing requirements for enzyme-substrate homology were exhibited by each of the three species of C3 and C5 convertases (C3 and C5 CVA). The results suggest that different strategies of molecular interaction evolved in complement systems of different species.
D000818:Animals; D001798:Blood Proteins; D050577:Complement C3-C5 Convertases; D003182:Complement C5; D003183:Complement C6; D003184:Complement C7; D003185:Complement C8; D003186:Complement C9; D003165:Complement System Proteins; D004285:Dogs; D004910:Erythrocyte Membrane / Q000276:immunology; D006168:Guinea Pigs; D006461:Hemolysis; D006801:Humans; D011817:Rabbits; D013045:Species Specificity
D001798:Blood Proteins; D003182:Complement C5; D003183:Complement C6; D003184:Complement C7; D003185:Complement C8; D003186:Complement C9; D003165:Complement System Proteins; D050577:Complement C3-C5 Convertases