Clusterin enhances the formation of insoluble immune complexes.
Clusterin was purified from human serum by sequential affinity chromatography over IgG-, protein A- and Con A-Sepharose. The protein was approximately 70 kDa by SDS/PAGE under nonreducing conditions and was resolved into approximately 35 kDa bands under reducing conditions. The protein reacted with clusterin-specific Mabs in ELISA and in Western blots. Its N-terminal sequences agreed with those published for clusterin. An antiserum specific for clusterin made by the above method detected it in complement membrane attack complexes on rabbit erythrocyte membranes. The interaction of clusterin with IgG was physiologically relevant because it was found to increase the rate of formation of insoluble immune complexes.
Wilson
M R
MR
Department of Biochemistry, University of Sydney, NSW, Australia.
Roeth
P J
PJ
Easterbrook-Smith
S B
SB
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000936:Antigen-Antibody Complex; D015153:Blotting, Western; D002846:Chromatography, Affinity; D051152:Clusterin; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007700:Kinetics; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D008970:Molecular Weight
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; C495242:CLU protein, human; D051152:Clusterin; D006023:Glycoproteins; D007074:Immunoglobulin G; D018832:Molecular Chaperones