Antibody to a cryptic, solid phase ClQ antigen in membranoproliferative nephritis View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1989-03

AUTHORS

C F Strife, A E Leahy, C D West

ABSTRACT

IgG containing material detected in membranoproliferative nephritis (MPGN) serum with a solid phase (sp) Clq ELISA has been presumed to be immune complexes. However, in serum from 13 MPGN patients containing large amounts of spClq-binding material, sucrose density ultracentrifugation and sieve chromatography showed spClq-binding protein to sediment at 7S or cofractionate with IgG. One serum (stored for 12 years) contained, in addition, spClq-binding material sedimenting at more than 19S. Isolated MPGN IgG was shown to bind to spClq. SpClq-binding material could be totally removed from MPGN serum by absorption with BSA-anti-BSA immune precipitates, and by acid elution of the precipitates IgG binding to spClq could be recovered. F(ab')2, isolated from pepsin digested MPGN IgG, continued to bind spClq. Binding of MPGN IgG or F(ab')2 to spClq was not inhibited by 2 M NaCl. Incubation of MPGN serum with 125I Clq followed by sucrose density ultracentrifugation resulted in a peak of radioactivity at 11S, the sedimentation rate of Clq, giving evidence that material binding fluid phase Clq is not present. SpClq-binding IgG was detected in 54% of 68 MPGN patients. These results indicate that the 7S spClq-binding IgG represents antibody to a cryptic antigen revealed only when Clq fixes to a solid surface. More... »

PAGES

836-842

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ki.1989.61

DOI

http://dx.doi.org/10.1038/ki.1989.61

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007838544

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2785226


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56 schema:description IgG containing material detected in membranoproliferative nephritis (MPGN) serum with a solid phase (sp) Clq ELISA has been presumed to be immune complexes. However, in serum from 13 MPGN patients containing large amounts of spClq-binding material, sucrose density ultracentrifugation and sieve chromatography showed spClq-binding protein to sediment at 7S or cofractionate with IgG. One serum (stored for 12 years) contained, in addition, spClq-binding material sedimenting at more than 19S. Isolated MPGN IgG was shown to bind to spClq. SpClq-binding material could be totally removed from MPGN serum by absorption with BSA-anti-BSA immune precipitates, and by acid elution of the precipitates IgG binding to spClq could be recovered. F(ab')2, isolated from pepsin digested MPGN IgG, continued to bind spClq. Binding of MPGN IgG or F(ab')2 to spClq was not inhibited by 2 M NaCl. Incubation of MPGN serum with 125I Clq followed by sucrose density ultracentrifugation resulted in a peak of radioactivity at 11S, the sedimentation rate of Clq, giving evidence that material binding fluid phase Clq is not present. SpClq-binding IgG was detected in 54% of 68 MPGN patients. These results indicate that the 7S spClq-binding IgG represents antibody to a cryptic antigen revealed only when Clq fixes to a solid surface.
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