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Registro Completo |
Biblioteca(s): |
Embrapa Meio Norte / UEP-Parnaíba. |
Data corrente: |
16/08/1996 |
Data da última atualização: |
16/08/1996 |
Autoria: |
PAPPENHEIMER, A. M.; OLSNES, S.; HARPER, A. A. |
Afiliação: |
Harvard University. |
Título: |
Lectins from abrus precatorius and ricinus communis.I.Immunochemical relationships between toxins and agglutinins. |
Ano de publicação: |
1974 |
Fonte/Imprenta: |
The Journal of Immunology, v.113, n.3, p.835-841, 1974. |
Idioma: |
Inglês |
Conteúdo: |
The quantitative precipitation reactions of rabbit anti-abrin and anti-ricin sera have been studied with the purified toxins, abrin, and ricin, their isolated A-and B-chains and with the corresponding nontoxic Abrus and Ricinus agglutinins. In the case of ricin, the results are consistent with a model in which the agglutinin contains two lactose-binding B-chains, immunologically indistinguishable from the single B-chain of ricin and two A-chains which lack certain antigenic determinants present on the ricin A-chain. The relative between abrin and its agglutinin appears basically similar, although somewhat more complex. Both Abrus and Ricinus lectins react with lactose and with glycoproteins containing terminal nonreducing galactose residues that are presenton certain proteins in the normal serum of many animal species and on the membranes of animal cells... |
Palavras-Chave: |
Lectin. |
Thesagro: |
Lectina; Ricinus Communis. |
Thesaurus Nal: |
Abrus precatorius. |
Categoria do assunto: |
-- |
Marc: |
LEADER 01439naa a2200193 a 4500 001 1078026 005 1996-08-16 008 1974 bl --- 0-- u #d 100 1 $aPAPPENHEIMER, A. M. 245 $aLectins from abrus precatorius and ricinus communis.I.Immunochemical relationships between toxins and agglutinins. 260 $c1974 520 $aThe quantitative precipitation reactions of rabbit anti-abrin and anti-ricin sera have been studied with the purified toxins, abrin, and ricin, their isolated A-and B-chains and with the corresponding nontoxic Abrus and Ricinus agglutinins. In the case of ricin, the results are consistent with a model in which the agglutinin contains two lactose-binding B-chains, immunologically indistinguishable from the single B-chain of ricin and two A-chains which lack certain antigenic determinants present on the ricin A-chain. The relative between abrin and its agglutinin appears basically similar, although somewhat more complex. Both Abrus and Ricinus lectins react with lactose and with glycoproteins containing terminal nonreducing galactose residues that are presenton certain proteins in the normal serum of many animal species and on the membranes of animal cells... 650 $aAbrus precatorius 650 $aLectina 650 $aRicinus Communis 653 $aLectin 700 1 $aOLSNES, S. 700 1 $aHARPER, A. A. 773 $tThe Journal of Immunology$gv.113, n.3, p.835-841, 1974.
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Embrapa Meio Norte / UEP-Parnaíba (CPAMN-UEPP) |
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