Isolation of immune complexes by an equine CIQ-like factor

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Abstract

A method for the isolation of circulating immune complexes by co-precipitation with an equine Clq-like factor is described. The Clq-like factor co-precipitated 80% of the 125I-labeled aggregated human IgG (AHG) following dialysis against 0.05 M Tris-HCl, pH 8.1 compared to only 2% of the unaggregated human IgG (HG). When incubated with bovine serum albumin (BSA) anti-BSA soluble immune complexes (IC) prepared at antigen (Ag)-antibody (Ab) equivalence or in Ab excess, the Clq-like factor co-precipitated 100Z of the available complexes. Under conditions of 2x Ag excess, Clq-like factor was less efficient as demonstrated by co-precipitation of 40% of the available IC. Although the nature and specificity of binding of the Clq-like factor is unknown, its isolation and partial characterization are reported.

Original languageEnglish (US)
Pages (from-to)741-752
Number of pages12
JournalImmunological Investigations
Volume10
Issue number8
DOIs
StatePublished - Jan 1 1981

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Antigen-Antibody Complex
Horses
Bovine Serum Albumin
Immunoglobulin G
Antigens
Antibodies
Dialysis

ASJC Scopus subject areas

  • Immunology

Cite this

Isolation of immune complexes by an equine CIQ-like factor. / Mcdonald, Thomas L.

In: Immunological Investigations, Vol. 10, No. 8, 01.01.1981, p. 741-752.

Research output: Contribution to journalArticle

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