Occurrence of -globulin complexes in serum and joint fluid of rheumatoid arthritis patients: use of monoclonal rheumatoid factors as reagents for their demonstration.
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gammaG globulin complexed in an unusual form has been demonstrated in the serum of many patients with rheumatoid arthritis. Such complexes have been detected and isolated principally through precipitation reactions with monoclonal gammaM rheumatoid factors. These monoclonal rheumatoid factors exhibited a greater sensitivity to react with small complexes or aggregates of gamma-globulin than polyclonal rheumatoid factor from rheumatoid arthritis sera or isolated C1q. The serum complexes consisted in large part of high molecular weight but acid-dissociable 7S gammaG globulin molecules They however differed from the complexes in the joint fluid by not yielding precipitates with C1q and were not found in association with evidence of marked serum complement fixation or activation. A small number of systemic lupus erythematosus sera, primarily those forming cryoprecipitates, also gave reactions with monoclonal rheumatoid factor. Sera from patients with a variety of nonrheumatic diseases gave a low incidence of reactions. The exact nature of the complexes in the rheumatoid arthritis sera remains somewhat in doubt although gammaG rheumatoid factors appear partly involved.Keywords:
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A comparative study of testing methods for polyclonal and monoclonal antibodies to human interferon using direct and reverse neutralization of the antiviral activity of interferon as well as ELISA was carried out. The activity of antibodies in ELISA was dozens of times higher than in neutralization tests. Polyclonal antibodies from the sera of mice immunized with alpha 2 interferon had a higher neutralizing capacity. M-5 monoclonal antibodies in specimens of ascitic fluid induced by inoculation of mice with hybrid cells exhibited an increase in both binding and neutralizing activity as compared with specimens of the culture fluid. Immunoglobulins from the ascitic and culture fluid of nonproductive myeloma cells as well as hybridomas producing monoclonal antibodies of other specificities showed practically no reaction with interferon in any of the tests under study. The screening of monoclonal antibodies intended for research and biotechnological purposes requires a composite analysis in both neutralization and binding tests in order to recover purposefully the hybrid clones producing antibodies with both or one of these properties.
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Abstract Monoclonal antibodies directed against sheep erythrocytes of the isotypes IgG 1 ,IgG 2b and IgG 2a were used to analyze the specificity of antibody‐induced suppression of the immune response. It was first shown that all monoclonals reacted against different antigenic determinants and they all suppressed the immune response to sheep erythrocytes when given shortly after the antigen to more than 50% as compared to 90–96% inhibition obtained with a polyclonal antiserum. Increasing the doses of monoclonals did not increase suppression. However, two different monoclonals administered together caused an additive, but not a synergistic inhibitory effect. No enhancement of the immune response was observed with any of the Ig classes tested. These findings show that four different antigenic determinants on sheep erythrocytes induced the synthesis of corresponding antibodies, with little or no signs of a dominant determinant. Passively administered monoclonal antibodies, even at supraoptimal doses, never suppressed the immune response to the same extent as a polyclonal antiserum, suggesting that each monoclonal only suppressed the synthesis of the corresponding antibody and did not affect antibody synthesis to other determinants.
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Cryoglobulins were studied in the sera of 40 unselected pSS patients. The nature of the cryoglobulins was defined using a very fast and sensitive resolution electrophoresis technique combined with immunofixation. Thirty-five per cent of SS patients were shown to have circulating IgMk mixed monoclonal cryoglobulins. On the contrary, all the other tested cryoprecipitates were found to be mixed polyclonal, with the exception of one patient with SLE. The presence of cryoglobulins in the sera of SS patients correlated with extraglandular disease and with autoantibodies to Ro (SSA) cellular antigen and rheumatoid factor. Patients with cryoglobulins had lower serum C4 levels compared to patients without cryoglobulins. These findings suggest that SS in addition to polyclonal B-cell hyperreactivity expresses a monoclonal process preceding the development of lymphoid neoplasia. Extraglandular manifestations of the syndrome may be associated with an immune complex mediated pathology.
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SUMMARY. To determine the basis of the tissue cross‐reactions shown by some human monoclonal anti‐Rh D antibodies, we have investigated the tissue reactivities of 48 further human monoclonal antibodies (mAb) against D and other Rh antigens, and compared them with those of normal and anti‐D sera and immunoglobulin preparations, and affinity‐purified polyclonal anti‐D antibodies. Although we were unable to detect any tissue reactivities associated with the D‐binding fraction of polyclonal antisera or prophylactic immunoglobulin, the non‐erythroid cell types identified by the tissue‐reactive human anti‐Rh mAb of both IgM and IgG class were those recognized by antibodies present in both normal and anti‐D sera. These results indicate: (a) that the tissue specificities of human anti‐Rh mAb are similar to those of natural antibodies, and (b) that there are immunochemical differences between polyclonal and monoclonal anti‐D antibodies, at least of IgG class, which may be relevant to the use of the latter in the prevention of haemolytic disease of the new‐born by immune prophylaxis.
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Abstract Monoclonal antibodies were produced against human angiotensinogen. An enzyme linked immunosorbent assay (ELISA) was developed using a high affinity monoclonal antibody as catching antibody and a polyclonal rabbit anti human agiotensinogen antibody as detecting antibody in a “sandwich” ELISA.
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Both human B cell hybridoma technology and convalescent plasma therapy are promising immunological tools for therapeutic interventions. Here we propose using antibody producing B cells from convalescent SARS-CoV2 patients for developing human B cell hybridomas, and a combination of monoclonal antibodies against multiple immunogenic targets of SARS-CoV-2 spike protein might deliver an antibody cocktail for long-lasting therapeutic targeting.
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Monoclonal immunoglobulins present a normal structure and have an antibody activity. This activity may be directed against exo-antigens especially bacterial, but more frequently against auto-antigens. It may then be symptomatic and therefore explain unusual clinical or biological manifestations in the course of monoclonal dysglobulinemias; but, most of the time, the monoclonal auto-antibody activity is asymptomatic and polyspecific, as it is only the monoclonal expression of polyclonal natural auto-antibodies. A comprehensive review of the various antibody activities of monoclonal immunoglobulins is presented. With the presence, in large quantities, of monoclonal immunoglobulins and their antibody activity, the links between dysglobulinemia and autoimmune disease are discussed as well as the pathogenic role of auto-antibodies.
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Objective: To screen monoclonal antibody against protein drugs bound with plasma protein in blood samples.Methods:After coated with rabbit anti-K102 polyclonal antibody purified by affinity chromatography,adding K102 antigen diluted with PBS containing 10% monkey plasma PBS and the supernatant of hybridoma and HRP-goat anti-mouse IgG are added to screen positive hybridoma lines which might produce monoclonal antibodies.Results:In use of the method of double-antibody sandwich ELISA screening,the six hybridoma lines are successfully screened to be capable of screening stably the antibody against K102,named as 1C9,2D7,3E2,5F4,5F6,6B9.The monoclonal antibodies could detect K102 concentration in the blood samples.Conclusion:The improved double-antibody sandwich ELISA can be used to screening hybridoma cell lines of monoclonal antibodies against biodrugs bound with plasma protein.
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