| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Meio Norte / UEP-Parnaíba. |
|
Data corrente: |
22/11/1995 |
|
Data da última atualização: |
22/11/1995 |
|
Autoria: |
CARLINI, C. R.; BARCELLOS, G. B. S.; BAETA-NEVES, A.D.V.; GUIMARAES, J. A. |
|
Afiliação: |
Universidade Federal do Rio de Janeiro. |
|
Título: |
Immunoreactivity for canatoxin and concanavalin a among proteins of leguminous seeds. |
|
Ano de publicação: |
1988 |
|
Fonte/Imprenta: |
Phytochemistry, v.27, n.1, p.25-30, 1988. |
|
Idioma: |
Inglês |
|
Conteúdo: |
The jack bean (Canavalia ensiformis) is the natural source of concanavalin A and also of canatoxin, a recently described neurotoxic protein. Among some other examples, the seeds of the euphorbiaceous plant Ricinus communis contain ricin, a toxic monovalent lectin, and also an agglutinin which are closely related molecules sharing a common polypeptide subunit. Thus, seeds containing two distinct and related proteins, an atoxic lectin and a highly toxic protein which behaves as an monovalent lectin or a hemilectin, seem to be widespread. In this paper we describe the simultaneous presence of both toxic proteins and lectins in the seed extracts of 13 out of 16 different leguminous plants examined. Immunodifusion studies with anticanatoxin and anticoncanavalinA IgG antibodies indicated that proteins structurally resembling canatoxin were preserved in almost all the leguminous seeds extract except in peanut and R. communis. Proteins immunogically related to concanavalin A were detected only for the Canavalia genus despite the ubiquitous presence of lectins in seeds. The data suggest that canatoxin-like proteins were conservatively preserved, indicating that this toxic protein as well as other toxic hemilectins may play an important physiological role in plants. |
|
Palavras-Chave: |
Canatoxin; Immunoreactivity; Imunoreatividade; Leguminous seeds; Proteina toxica; Sementes leguminosas; Toxic protein. |
|
Thesagro: |
Lectina. |
|
Thesaurus Nal: |
concanavalin A; lectins. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 02035naa a2200277 a 4500
001 1075355
005 1995-11-22
008 1988 bl --- 0-- u #d
100 1 $aCARLINI, C. R.
245 $aImmunoreactivity for canatoxin and concanavalin a among proteins of leguminous seeds.
260 $c1988
520 $aThe jack bean (Canavalia ensiformis) is the natural source of concanavalin A and also of canatoxin, a recently described neurotoxic protein. Among some other examples, the seeds of the euphorbiaceous plant Ricinus communis contain ricin, a toxic monovalent lectin, and also an agglutinin which are closely related molecules sharing a common polypeptide subunit. Thus, seeds containing two distinct and related proteins, an atoxic lectin and a highly toxic protein which behaves as an monovalent lectin or a hemilectin, seem to be widespread. In this paper we describe the simultaneous presence of both toxic proteins and lectins in the seed extracts of 13 out of 16 different leguminous plants examined. Immunodifusion studies with anticanatoxin and anticoncanavalinA IgG antibodies indicated that proteins structurally resembling canatoxin were preserved in almost all the leguminous seeds extract except in peanut and R. communis. Proteins immunogically related to concanavalin A were detected only for the Canavalia genus despite the ubiquitous presence of lectins in seeds. The data suggest that canatoxin-like proteins were conservatively preserved, indicating that this toxic protein as well as other toxic hemilectins may play an important physiological role in plants.
650 $aconcanavalin A
650 $alectins
650 $aLectina
653 $aCanatoxin
653 $aImmunoreactivity
653 $aImunoreatividade
653 $aLeguminous seeds
653 $aProteina toxica
653 $aSementes leguminosas
653 $aToxic protein
700 1 $aBARCELLOS, G. B. S.
700 1 $aBAETA-NEVES, A.D.V.
700 1 $aGUIMARAES, J. A.
773 $tPhytochemistry$gv.27, n.1, p.25-30, 1988.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Meio Norte / UEP-Parnaíba (CPAMN-UEPP) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
| Registros recuperados : 140 | |
| Registros recuperados : 140 | |
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
