| Literature DB >> 2742403 |
M W Robinson1, D G Scott, P A Bacon, K W Walton, J S Coppock, D L Scott.
Abstract
The proteins present in 4% polyethylene glycol (PEG) precipitates of 10 normal sera and 60 samples from patients with rheumatic diseases were studied. A variety of immunochemical methods were used, including estimation of the percentages of total serum proteins precipitated by PEG, gel filtration analyses of the precipitates, and affinity chromatography with protein A and anti-immunoglobulin columns. Substantial amounts of protein were precipitated from normal sera. Many non-immunoglobulin proteins were precipitated from patients' sera, including fibronectin, haptoglobin, albumin, transferrin, and alpha 1-antitrypsin. Affinity chromatography with anti-immunoglobulin columns bound non-immunoglobulin proteins from PEG precipitates, but the protein A affinity column did not do so. The view that circulating antibody-antigen complexes alone are precipitated by 4% PEG is too simplistic; many non-immunoglobulin proteins are involved. They may either bind to immune complexes or be coprecipitated owing to non-specific protein aggregation.Entities:
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Year: 1989 PMID: 2742403 PMCID: PMC1003794 DOI: 10.1136/ard.48.6.496
Source DB: PubMed Journal: Ann Rheum Dis ISSN: 0003-4967 Impact factor: 19.103