[Binding and activation of the first component of human complement on artificial matrices].
Artificial sorbents that comprise macroporous glass covered by the copolymer of N-vinylpyrrolidone and N-substituted acrylamide have been synthesized. Aminoethanol is bound to acrylic acid residue in one sorbent (AE-glass), whereas the other sorbent involves immunoglobulin G with the hexamethylenediamine spacer (IgG-glass). C1q binds specifically to IgG-glass with Ka 4,07(+/- 0,32) X 10(7) M-1. Free energy of the C1q binding to IgG-glass is twice higher than that of its binding to monomeric IgG. This evidences that one C1q molecule associates with two IgG molecules of the sorbent. A weak nonspecific sorption of C1q to AE-glass was found. Both specific (on IgG-glass) and nonspecific (on AE-glass) sorption of the first component of complement activate the classical pathway in human serum as manifested in the consumption of the C4, C2, C3 and C5 components. IgG-glass was employed for C1q isolation from human serum by affinity chromatography, whereas unbound part of serum may be used as a reagent R1q. The yield of highly purified C1q after IgG-glass affinity chromatography and gel filtration on Sephacryl S-300 is 63,6%.
D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003167:Complement Activation; D003172:Complement C1 / Q000302:isolation & purification / Q000378:metabolism*; D003171:Complement Pathway, Classical; D005898:Glass; D006801:Humans; D066298:In Vitro Techniques
D003172:Complement C1
Sviazyvanie i aktivatsiia pervogo komponenta komplementa cheloveka na iskusstvennykh matritsakh.