Stoichiometry and sedimentation properties of the complex formed between the C1q and C1r2C1s2 subcomponents of the first component of complement.
We have examined the functional and hydrodynamic properties of the first component of human complement, C1, and the activated first component, C1-, reassembled in the presence of Ca++ from C1q and either the C1r2C1s2 or the C1r-2C1s-2 tetramer. Reconstituted C1 has hemolytic activity similar to C1 in serum. As long as either tetramer is in excess and the total concentration is low, we find that only a 1:1 complex is formed between C1q and either the unactivated or activated tetramer. This complex sediments at 15.9 +/- 0.2 Svedbergs and has a complex sediments at 15.9 +/- 0.2 Svedbergs and has a m.w. of 739,000 +/- 37,000. The boundary shape of the sedimenting C1- preparation was broader than that of C1 suggesting the association constant between C1r2C1s2 and C1q may have decreased upon activation. At elevated concentrations, with more than a molar excess of C1q, C1 aggregated to form both 16S and 23S species.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003166:Complement Activating Enzymes; D003172:Complement C1 / Q000145:classification*; D015922:Complement C1q; D006461:Hemolysis; D006801:Humans; D046911:Macromolecular Substances; D008433:Mathematics; D008970:Molecular Weight; D011817:Rabbits; D012756:Sheep; D014461:Ultracentrifugation
D003172:Complement C1; D046911:Macromolecular Substances; D015922:Complement C1q; D003166:Complement Activating Enzymes