Fluid phase destruction of C2hu by C1hu. II. Unmasking by C4ihu of C1hu specificity for C2hu.
It has been demonstrated that C1 isolated in the unactivated form fails to inactivate C4 or C2 in the fluid phase, while the activated molecule, C1 rapidly converts C4 to hemolytically inactive C4i, but does not efficiently inactivate C2. The production and presence of C4i now confers on C1 the ability to rapidly inactivate C2. After heating at 56 degrees C, so as to destroy the hemolytic activity, heat inactivated C1 is still capable of inactivating C4 but the presence of C4i no longer confers an ability to inactivate C2. Studies with the subunits of C1-C1q, C1r, C1s, indicate that the action of C1s on C2 can be inhibited by C1r and that this inhibition is reversed by the presence of homologous C4. These studies indicate that the interaction of C4i with a heat labile receptor conformation in C1 uncovers a masked specificity for C2.
D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003169:Complement Inactivator Proteins; D003165:Complement System Proteins; D006168:Guinea Pigs; D006461:Hemolysis; D006358:Hot Temperature; D006801:Humans; D007122:Immunoelectrophoresis; D007700:Kinetics; D013045:Species Specificity; D013451:Sulfonic Acids / Q000494:pharmacology
D003169:Complement Inactivator Proteins; D013451:Sulfonic Acids; D003165:Complement System Proteins