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Analogous antigenic alterations elicited in C3 by physiologic binding and by denaturation in the presence of sodium dodecylsulfate.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Oncology, Radiology and Clinical Immunology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Oncology, Radiology and Clinical Immunology. (Nilsson Bo)
1982 (English)In: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 129, no 6, 2594-2597 p.Article in journal (Refereed) Published
Abstract [en]

The expression of three antigenic subsets of C3--the C3(S), the C3(N), and the C3(D) antigens--by soluble and target-bound forms of C3 was studied. The C3(S) subset is stable and is expressed by native as well as denatured C3 (exposure to sodium dodecyl sulphate (SDS) M greater than or equal to 10(-3)). The C3(N) and C3(D) subsets are labile and are expressed by native and denatured C3, respectively. Antisera to native C3, anti-C3(S-N), react with the C3(S) as well as the C3(N) subset. Antisera to isolated C3 subunits react exclusively with the C3(D) subset. A separation of anti-C3(S) and anti-C3(N) antibodies was accomplished by adsorbing the anti-C3(S-N) antiserum with insolubilized, denatured C3, anti-C3(N) antibodies remained unadsorbed. Anti-C3(S) antibodies were adsorbed and subsequently eluted from the denatured C3. Agglutination studies with EAC1423b cells showed significant agglutination with anti-C3(S) and anti-C3(D) antisera but reduced agglutination with anti-C3(N) antisera. Agglutination by anti-C3(D) antisera was unaffected in the presence of EDTA serum containing converted or unconverted C3. These data suggest an antigenic modification of C3b-b' upon binding that mirrors the antigenic transition associated with SDS denaturation of C3.

Place, publisher, year, edition, pages
1982. Vol. 129, no 6, 2594-2597 p.
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Other Medical Sciences
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URN: urn:nbn:se:uu:diva-265359PubMedID: 6183339OAI: oai:DiVA.org:uu-265359DiVA: diva2:865261
Available from: 2015-10-27 Created: 2015-10-27 Last updated: 2017-12-01

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