Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin
olecular parameters controlling antigenicity* that is immunogenialty and antigenic specificity, are reviewed together with acme aspects of humoral immunity and tolerance, and characteristics and functions of cells involved in these immunological phenomena* Antigenicity of native monomer, heat-denatu...
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ndltd-bl.uk-oai-ethos.bl.uk-6575222018-10-09T03:23:44ZImmunogenicity and antigenic specificity of monomer and polymers of bovine serum albuminStrambachova-McBride, Jana1975olecular parameters controlling antigenicity* that is immunogenialty and antigenic specificity, are reviewed together with acme aspects of humoral immunity and tolerance, and characteristics and functions of cells involved in these immunological phenomena* Antigenicity of native monomer, heat-denatured monomer and heatpolymerised bovine serum albumin (BSA) have been compared. Both aonooeric antigens were similar in the three aspects of antigenicity examined, namely their humoral iraaunogenicity, tolerogenicity and serological specificity. The antigenicity of polymerised BSA differed from that of monomers in both its imaunogenlcity and serological behaviour. Polymerised BSA Induced stronger primary and secondary humoral responses of anti-native specificity than did the monomers in both mice and rabbits. The apparent immunogenic (priming) threshold dose of polymerised BSA was approximately ten fold lower than that of monomer in CM mice. Partial humoral tolerance (low-gone) was induced by all three BSA antigens in CBA mice. The threshold tolerogenic dose was essentially the same (lpg) for monomer and polymerized BSA. The hyporespemsiveness induced by polymerised BSA was both leas pronounced and more transient than that due to monomer. Serological activity of the BSA antigens was examined by a primary binding assay of Parr. Distinct differences between monomelic and polymerized BSA were observed with respect to the slope of their binding curves, association and dissociation rates of their binding to antibody, and mutual cross-reactivity in an inhibition assay. The results of the serological studies could be attributed to either a new specificity or, store comprehensively, to an enhanced capacity of polymerised BSA to establish avid bonds with antibody* The polymerised B3A was removed from circulation of CBA mice more rapidly than were the momwers* However, a large proportion of polymerised BSA was released in a little degraded form from peritoneal exudate cells cultured in vitro after the uptake* A possible relationship between the serological and immunogenic properties of the BSA antigens, as well as the significance of their handling by phagocytic cells, were discussed.571.96University of Edinburghhttps://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.657522http://hdl.handle.net/1842/26982Electronic Thesis or Dissertation |
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571.96 Strambachova-McBride, Jana Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
description |
olecular parameters controlling antigenicity* that is immunogenialty and antigenic specificity, are reviewed together with acme aspects of humoral immunity and tolerance, and characteristics and functions of cells involved in these immunological phenomena* Antigenicity of native monomer, heat-denatured monomer and heatpolymerised bovine serum albumin (BSA) have been compared. Both aonooeric antigens were similar in the three aspects of antigenicity examined, namely their humoral iraaunogenicity, tolerogenicity and serological specificity. The antigenicity of polymerised BSA differed from that of monomers in both its imaunogenlcity and serological behaviour. Polymerised BSA Induced stronger primary and secondary humoral responses of anti-native specificity than did the monomers in both mice and rabbits. The apparent immunogenic (priming) threshold dose of polymerised BSA was approximately ten fold lower than that of monomer in CM mice. Partial humoral tolerance (low-gone) was induced by all three BSA antigens in CBA mice. The threshold tolerogenic dose was essentially the same (lpg) for monomer and polymerized BSA. The hyporespemsiveness induced by polymerised BSA was both leas pronounced and more transient than that due to monomer. Serological activity of the BSA antigens was examined by a primary binding assay of Parr. Distinct differences between monomelic and polymerized BSA were observed with respect to the slope of their binding curves, association and dissociation rates of their binding to antibody, and mutual cross-reactivity in an inhibition assay. The results of the serological studies could be attributed to either a new specificity or, store comprehensively, to an enhanced capacity of polymerised BSA to establish avid bonds with antibody* The polymerised B3A was removed from circulation of CBA mice more rapidly than were the momwers* However, a large proportion of polymerised BSA was released in a little degraded form from peritoneal exudate cells cultured in vitro after the uptake* A possible relationship between the serological and immunogenic properties of the BSA antigens, as well as the significance of their handling by phagocytic cells, were discussed. |
author |
Strambachova-McBride, Jana |
author_facet |
Strambachova-McBride, Jana |
author_sort |
Strambachova-McBride, Jana |
title |
Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
title_short |
Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
title_full |
Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
title_fullStr |
Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
title_full_unstemmed |
Immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
title_sort |
immunogenicity and antigenic specificity of monomer and polymers of bovine serum albumin |
publisher |
University of Edinburgh |
publishDate |
1975 |
url |
https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.657522 |
work_keys_str_mv |
AT strambachovamcbridejana immunogenicityandantigenicspecificityofmonomerandpolymersofbovineserumalbumin |
_version_ |
1718771867254259712 |