Registro Completo
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Biblioteca(s): |
Embrapa Agrobiologia. |
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Data corrente: |
15/03/1999 |
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Data da última atualização: |
15/03/1999 |
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Autoria: |
OLIVEIRA, A. L. B.; RIBEIRO, J. R. A.; RUMJANEK, V. M.; RUMJANEK, Norma G. |
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Título: |
Antisera protein a purification improve the specificity of recognition of Bradyrhizobium polysaccharides. |
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Ano de publicação: |
1997 |
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Fonte/Imprenta: |
In: REUNIAO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUIMICA E BIOLOGIA MOLECULAR, 26., maio 1997, Caxambu. Resumos... Caxambu: Sociedade Brasileira de Bioquimica e Biologia Molecular, 1997. p.135. |
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Idioma: |
Inglês |
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Conteúdo: |
Crossreaction is a major problem for immunological studies when de polyclonal serum is used. The presence of another immunoglobulins than IgG results in the recognition of another molecules than the specifics antigens. The protein A purification of antiserum has been reported as an excelent method to isolate igG of other serum proteins. This purification improves the reaction and the specificity of antisera which are used in immunological studies of Rhizobia. This studies include identification and competitive assays of bacteria and surface molecules. Rhizobia are gram-negative symbiotic nitrogen fixing bacteria which infect the roots of leguminous plants and have on their surface a high amount of polysaccharides, which may comprise the following types: exo- polysaccharides (EPS), capsular polysaccharide (CPS), lipopolysaccharide (LPS) and B-glucans. Several functions have already been suggested for polysaccharides, regarding the infection process, nodulation and nitrogen-fixing efficiency. In this work we tested the reactivity and the specificity of two purified and unpurified sera(antiBR-33 strain of B. japonicum and antiBR-96 strain of B. elkanii) with EPS and CPS. The unpurified sera showed intense nonespecific recognition. The responses were similar for both types of polysaccharide although the CPS reactions were slightly more intense. The cross-reactions were extremely reduced and even eliminated by purification of the sera. The present work showed that purification with protein A improves the... MenosCrossreaction is a major problem for immunological studies when de polyclonal serum is used. The presence of another immunoglobulins than IgG results in the recognition of another molecules than the specifics antigens. The protein A purification of antiserum has been reported as an excelent method to isolate igG of other serum proteins. This purification improves the reaction and the specificity of antisera which are used in immunological studies of Rhizobia. This studies include identification and competitive assays of bacteria and surface molecules. Rhizobia are gram-negative symbiotic nitrogen fixing bacteria which infect the roots of leguminous plants and have on their surface a high amount of polysaccharides, which may comprise the following types: exo- polysaccharides (EPS), capsular polysaccharide (CPS), lipopolysaccharide (LPS) and B-glucans. Several functions have already been suggested for polysaccharides, regarding the infection process, nodulation and nitrogen-fixing efficiency. In this work we tested the reactivity and the specificity of two purified and unpurified sera(antiBR-33 strain of B. japonicum and antiBR-96 strain of B. elkanii) with EPS and CPS. The unpurified sera showed intense nonespecific recognition. The responses were similar for both types of polysaccharide although the CPS reactions were slightly more intense. The cross-reactions were extremely reduced and even eliminated by purification of the sera. The present work showed that purification w... Mostrar Tudo |
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Palavras-Chave: |
Antigen antibody reaction; Reacao antigeno. |
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Thesagro: |
Anticorpo; Imunidade; Polissacarídeo; Proteína. |
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Thesaurus NAL: |
Bradyrhizobium; immunity; polysaccharides; proteins. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02452naa a2200277 a 4500
001 1620983
005 1999-03-15
008 1997 bl uuuu u00u1 u #d
100 1 $aOLIVEIRA, A. L. B.
245 $aAntisera protein a purification improve the specificity of recognition of Bradyrhizobium polysaccharides.
260 $c1997
520 $aCrossreaction is a major problem for immunological studies when de polyclonal serum is used. The presence of another immunoglobulins than IgG results in the recognition of another molecules than the specifics antigens. The protein A purification of antiserum has been reported as an excelent method to isolate igG of other serum proteins. This purification improves the reaction and the specificity of antisera which are used in immunological studies of Rhizobia. This studies include identification and competitive assays of bacteria and surface molecules. Rhizobia are gram-negative symbiotic nitrogen fixing bacteria which infect the roots of leguminous plants and have on their surface a high amount of polysaccharides, which may comprise the following types: exo- polysaccharides (EPS), capsular polysaccharide (CPS), lipopolysaccharide (LPS) and B-glucans. Several functions have already been suggested for polysaccharides, regarding the infection process, nodulation and nitrogen-fixing efficiency. In this work we tested the reactivity and the specificity of two purified and unpurified sera(antiBR-33 strain of B. japonicum and antiBR-96 strain of B. elkanii) with EPS and CPS. The unpurified sera showed intense nonespecific recognition. The responses were similar for both types of polysaccharide although the CPS reactions were slightly more intense. The cross-reactions were extremely reduced and even eliminated by purification of the sera. The present work showed that purification with protein A improves the...
650 $aBradyrhizobium
650 $aimmunity
650 $apolysaccharides
650 $aproteins
650 $aAnticorpo
650 $aImunidade
650 $aPolissacarídeo
650 $aProteína
653 $aAntigen antibody reaction
653 $aReacao antigeno
700 1 $aRIBEIRO, J. R. A.
700 1 $aRUMJANEK, V. M.
700 1 $aRUMJANEK, Norma G.
773 $tIn: REUNIAO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUIMICA E BIOLOGIA MOLECULAR, 26., maio 1997, Caxambu. Resumos... Caxambu: Sociedade Brasileira de Bioquimica e Biologia Molecular, 1997. p.135.
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Registro original: |
Embrapa Agrobiologia (CNPAB) |
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