Binding of isolated rheumatoid factors to histone proteins and basic polycations.
Open Access
- 1 August 1983
- journal article
- research article
- Published by BMJ in Annals Of The Rheumatic Diseases
- Vol. 42 (4), 435-438
- https://doi.org/10.1136/ard.42.4.435
Abstract
A fluorimetric immunoassay has been used to assess reactivity of rheumatoid factor (RF) with both histone proteins and other basic polycations (poly-L-lysine, poly-L-ornithine, and protamine) bound to an immobilised tyrosine-glutamic acid polyanionic copolymer. Isolated RF preparations can bind to histone proteins in this assay, notably to H3 and H4 histones, and this activity was always masked in the original whole seropositive sera. Binding of isolated RF was often noted also to the other large-molecular-weight basic polycations.This publication has 11 references indexed in Scilit:
- IgM-rheumatoid factors cross-reactive with IgG and a cell nuclear antigen: immunopathological implications?Annals Of The Rheumatic Diseases, 1980
- Evidence for a subset of rheumatoid factors that cross-react with DNA-histone and have a distinct cross-idiotype.The Journal of Experimental Medicine, 1980
- Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength.Proceedings of the National Academy of Sciences, 1979
- IgM‐Rheumatoid Factors Cross‐reactive with IgG and a Cell Nuclear Antigen: Apparent ‘Masking’ in Original SerumScandinavian Journal of Immunology, 1979
- Electrophoretic desorption of immunoglobulins from immobilised protein A and other ligandsJournal of Immunological Methods, 1978
- Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNANature, 1978
- Certain rheumatoid factors react with nucleosomesNature, 1978
- Estimation of IgM rheumatoid factors by fluorimetry.Annals Of The Rheumatic Diseases, 1978
- Certain Rheumatoid Factors React with both IgG and an Antigen Associated with Cell NucleiScandinavian Journal of Immunology, 1978
- Chapter 11 The Isolation and Purification of HistonesMethods in Cell Biology, 1977