Dissociation of primary antigen-antibody bonds is essential for complement mediated solubilization of immune precipitates.
The role of dissociation of primary antigen-antibody bonds in the solubilization of immune complexes (IC) has been investigated using photo-affinity crosslinked IC comprising NAP15-BSA and murine monoclonal anti-DNP antibodies. Non-covalently linked IC were solubilized rapidly when incubated with normal human serum (NHS), whereas covalently-linked IC were solubilized poorly or not at all. The rate and extent of complement activation produced by incubating covalently-linked and non-covalently linked IC with NHS was similar as assessed by the production of the C1s:C1-inhibitor, C3:properdin and C5b-9 complexes and the anaphylatoxins C4a and C3a. Thus, the inability of serum to solubilize photo-affinity crosslinked IC must be due to failure of dissociation of primary antigen-antibody bonds.
Johnston
A
A
University Department of Pathology, Western Infirmary, Glasgow, U.K.
Auda
G R
GR
Kerr
M A
MA
Steward
M W
MW
Whaley
K
K
D000818:Animals; D000936:Antigen-Antibody Complex / Q000737:chemistry*; D003167:Complement Activation; D003165:Complement System Proteins / Q000502:physiology*; D051379:Mice; D012995:Solubility
D000936:Antigen-Antibody Complex; D003165:Complement System Proteins