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Registro Completo |
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Biblioteca(s): |
Embrapa Pantanal. |
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Data corrente: |
16/01/2001 |
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Data da última atualização: |
12/04/2017 |
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Autoria: |
ANDREOTTI, R.; ARAUJO, M. S.; SAMPAIO, C. A. M.; CHUDZINSKI, A. M.; SAMPAIO, M. U. |
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Afiliação: |
EMBRAPA Pantanal (Corumba, MS). Instituto Butanta. Escola Paulista de Medicina (Sao Paulo, SP). |
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Título: |
Kininogens in plasma of Caiman (Caiman crocodilus yacare). |
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Ano de publicação: |
1991 |
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Fonte/Imprenta: |
In: REUNIAO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUIMICA E BIOLOGIA MOLECULAR, 20., 1991, Caxambu. Resumos. Caxambu: [s.n.], 1991. p.287. |
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Idioma: |
Inglês |
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Conteúdo: |
Kininogens are the major mammalian plasma cysteine proteinase inhibitors; a kininogen-like protein was also found in Bothrops jararaca (poisonous snake) plasma. The objetive of this communication is to describe a kininogen like protein in plasma of Caiman crocodilus yacare. Total caiman plasma protein is in range of 80 mg/ml. Caiman crude plasma, like snakes, does not contain detectable quantities of cysteine proteinase inhibitors, but following an ion-exchange chromatography of crude plasma on a DEAE-Sephadex colum (0.1 M tris-HC1, pH 8.0 buffer), a protein eluted with 0.3 M NaCl strongly inhibited papain. The inhibitor was further purified by affinity chromatography on a carboxy-methylated-papain-Sepharose column. the molecular weight of the caiman cysteine proteinase inhibitor is in range of 70,000. The described properties of the isolated caiman protein indicate that a kininogen-like protein is a general finding in reptile plasma. The prothombin time (PT) and activated partial thromboplastin time (APTT) is higher when compared to human plasma. Caiman plasma also contains a trypsin inhibitory activity, but total inhibition of trypsin was not achieved. Reptilian kininogen may lack the site for interactin with plasma prokallikrein, and the sequence of the released kinin must be distinct from bradykini. The poor effectiveness of bradykinin on snake smooth muscle indicates that the reptile kinin receptors are adapted to the release of a reptile kinin. |
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Palavras-Chave: |
Caiman crocodilus yacare; Kininogens; Reptile. |
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Thesagro: |
Bioquímica; Jacaré; Plasma; Réptil. |
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Thesaurus Nal: |
biochemistry. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02242naa a2200265 a 4500
001 1804791
005 2017-04-12
008 1991 bl --- 0-- u #d
100 1 $aANDREOTTI, R.
245 $aKininogens in plasma of Caiman (Caiman crocodilus yacare).
260 $c1991
520 $aKininogens are the major mammalian plasma cysteine proteinase inhibitors; a kininogen-like protein was also found in Bothrops jararaca (poisonous snake) plasma. The objetive of this communication is to describe a kininogen like protein in plasma of Caiman crocodilus yacare. Total caiman plasma protein is in range of 80 mg/ml. Caiman crude plasma, like snakes, does not contain detectable quantities of cysteine proteinase inhibitors, but following an ion-exchange chromatography of crude plasma on a DEAE-Sephadex colum (0.1 M tris-HC1, pH 8.0 buffer), a protein eluted with 0.3 M NaCl strongly inhibited papain. The inhibitor was further purified by affinity chromatography on a carboxy-methylated-papain-Sepharose column. the molecular weight of the caiman cysteine proteinase inhibitor is in range of 70,000. The described properties of the isolated caiman protein indicate that a kininogen-like protein is a general finding in reptile plasma. The prothombin time (PT) and activated partial thromboplastin time (APTT) is higher when compared to human plasma. Caiman plasma also contains a trypsin inhibitory activity, but total inhibition of trypsin was not achieved. Reptilian kininogen may lack the site for interactin with plasma prokallikrein, and the sequence of the released kinin must be distinct from bradykini. The poor effectiveness of bradykinin on snake smooth muscle indicates that the reptile kinin receptors are adapted to the release of a reptile kinin.
650 $abiochemistry
650 $aBioquímica
650 $aJacaré
650 $aPlasma
650 $aRéptil
653 $aCaiman crocodilus yacare
653 $aKininogens
653 $aReptile
700 1 $aARAUJO, M. S.
700 1 $aSAMPAIO, C. A. M.
700 1 $aCHUDZINSKI, A. M.
700 1 $aSAMPAIO, M. U.
773 $tIn: REUNIAO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUIMICA E BIOLOGIA MOLECULAR, 20., 1991, Caxambu. Resumos. Caxambu: [s.n.], 1991. p.287.
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Registro original: |
Embrapa Pantanal (CPAP) |
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| Registros recuperados : 9 | |
| 7. |  | ANDREOTTI, R.; GOMES, A.; TORQUATO, R. J. S.; SAMPAIO, C. A. M.; TANAKA, A. S. Purificacao parcial de um inibidor de serinoproteases extraido de larva de carrapato Boophilus microplus. In : SEMINARIO BRASILEIRO DE PARASITOLOGIA VETERINARIA, 10.; SEMINARIO DE PARASITOLOGIA VETERINARIA DO MERCOSUL, 1., 1997, Itajai. Anais... Revista Brasileira de Parasitologia Veterinaria, Sao Paulo, v.6, n.2, p. 96, ago. 1997. Suplemento 1. Resumo A54. CNPGC.| Biblioteca(s): Embrapa Gado de Corte. |
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| 8. | | GOMES, A.; ANDREOTTI, R.; PIRES, P. P.; TANAKA, A. S.; TORQUATO, R. J. S.; SAMPAIO, C. A. M. Influencia da proteina Ibmti sobre o desenvolvimento e a progenie do Boophilus microplus. Estudo piloto. In: SEMINARIO BRASILEIRO DE PARASITOLOGIA VETERINARIA, 11.; SEMINARIO DE PARASITOLOGIA VETERINARIA DOS PAISES DO MERCOSUL, 2.; SIMPOSIO DE CONTROLE INTEGRADO DE PARASITOS DE BOVINOS, 1., 1999, Salvador. Anais... Ilheus: Colegio Brasileiro de Parasitologia Veterinaria, [1999?]. p.75. CNPGC. Resumo. TL-AB-213.| Biblioteca(s): Embrapa Gado de Corte. |
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| 9. | | ESPÍRITO SANTO, M. M.; SEVILHA, A. C.; ANAYA, F. C.; BARBOSA, R.; FERNANDES, G. W.; SANCHEZ AZOFEIFA, G. A.; SCARIOT, A.; NORONHA, S. E. D.; SAMPAIO, C. A. Sustainability of tropical dry forests: two case studies in southeastern and central brazil. Forest Ecology and Management, v. 258, p. 922-930, 2009.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| Registros recuperados : 9 | |
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