Show simple item record

dc.contributor.authorCooper, K M
dc.contributor.authorMoore, Michael
dc.date.accessioned2015-01-02T15:45:03Z
dc.date.available2015-01-02T15:45:03Z
dc.date.issued1983-06-10
dc.identifier.citationCritical aspects of immune complex assays employing polyethylene glycol. 1983, 60 (3):289-303 J Immunol Methodsen
dc.identifier.issn0022-1759
dc.identifier.pmid6602185
dc.identifier.urihttp://hdl.handle.net/10541/337762
dc.description.abstractTreatment of artificial immune complexes (ICs) with 2.5% polyethylene glycol (PEG)--conditions under which C1q-binding activity is routinely measured in the fluid phase--produced marked changes in molecular size as determined by Sepharose 6B chromatography. The effect of PEG on the C1q-binding capacity of ICs, was therefore investigated using a solid phase (SP) system. PEG enhanced the binding of aggregated human gammaglobulin (AHG) and artificial ICs to SP-C1q and, in reverse experiments, also increased the binding of C1q to SP-AHG. The degree of enhancement varied according to the Ag:Ab ratio employed; the binding of ICs formed in moderate Ab excess was only modestly enhanced but that of complexes formed at slight Ab excess, equivalence and Ag excess was markedly elevated. The profile of PEG-induced enhancement of binding paralleled that of similar ICs in the C1q fluid phase system, suggesting that C1q binding in the latter may be influenced by PEG. However, the C1q-binding activity of in vivo-formed ICs seemed to be relatively unaffected by PEG since enhanced binding was comparable in control and pathological sera. The results indicate that PEG causes cross-linking and aggregation of ICs (and possibly other serum proteins) which may alter their biological activity and hence influence the results of IC assays that employ this agent.
dc.language.isoenen
dc.rightsArchived with thanks to Journal of immunological methodsen
dc.subject.meshAntigen-Antibody Complex
dc.subject.meshChromatography, Gel
dc.subject.meshColonic Neoplasms
dc.subject.meshComplement Activating Enzymes
dc.subject.meshComplement C1q
dc.subject.meshHumans
dc.subject.meshPolyethylene Glycols
dc.subject.meshRectal Neoplasms
dc.titleCritical aspects of immune complex assays employing polyethylene glycol.en
dc.typeArticleen
dc.contributor.departmentDivision of Immunology, Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BXen
dc.identifier.journalJournal of Immunological Methodsen
html.description.abstractTreatment of artificial immune complexes (ICs) with 2.5% polyethylene glycol (PEG)--conditions under which C1q-binding activity is routinely measured in the fluid phase--produced marked changes in molecular size as determined by Sepharose 6B chromatography. The effect of PEG on the C1q-binding capacity of ICs, was therefore investigated using a solid phase (SP) system. PEG enhanced the binding of aggregated human gammaglobulin (AHG) and artificial ICs to SP-C1q and, in reverse experiments, also increased the binding of C1q to SP-AHG. The degree of enhancement varied according to the Ag:Ab ratio employed; the binding of ICs formed in moderate Ab excess was only modestly enhanced but that of complexes formed at slight Ab excess, equivalence and Ag excess was markedly elevated. The profile of PEG-induced enhancement of binding paralleled that of similar ICs in the C1q fluid phase system, suggesting that C1q binding in the latter may be influenced by PEG. However, the C1q-binding activity of in vivo-formed ICs seemed to be relatively unaffected by PEG since enhanced binding was comparable in control and pathological sera. The results indicate that PEG causes cross-linking and aggregation of ICs (and possibly other serum proteins) which may alter their biological activity and hence influence the results of IC assays that employ this agent.


This item appears in the following Collection(s)

Show simple item record