Functional properties of the allotypes of mouse complement regulatory protein, factor H: difference of compatibility of each allotype with human factor I.

摘要: Abstract Three allotypes of mouse factor H, H.1, H.2, and H.3 were purified from the sera mice with different H allotypes, their functional properties investigated. The three all bound to heparin, DNA, Con A, methylamine-treated C3 (C3(MA)mo) similar affinities for each protein immobilized, showed identical mobilities on SDS-PAGE, reacted well rabbit polyclonal antibody against H. 1 H.2. Factor I-cofactor activity these was measured using highly material mouse, guinea-pig, human origin. In a homologous system, expressed indistinguishable I (Imo)-cofactor cleavage C3(MA)mo. Imo-cofactor again in when (C3(MA)hu) or methylaminetreated guinea-pig (C3(MA)gp) substituted C3(MA)mo substrate. cofactor however, augmented 4–5 times if C3(MA)hu used instead C3(MA)mo, barely detected C3(MA)gp employed. contrast, differences potency revealed (Ihu) Imo: order efficiency H.2 > = H.3. These results, taken together finding that combinations factors greater than did heterologous I, suggest discriminate species protease but not those substrate C3(MA), possesses best compatibility Ihu inactivation.