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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
17/11/2022 |
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Data da última atualização: |
01/12/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
FELICIANO, G. P.; ARIMORI, S. H.; NAKAO, V. W.; SANTOS, J. R. dos; MARTINS, E. A. L.; BEMQUERER, M. P.; CHENG, M. |
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Afiliação: |
GABRIEL PINNA FELICIANO, Instituto Butantan; SARA HAYAMA ARIMORI, Instituto Butantan; VINICIUS WATANABE NAKAO, Instituto Butantan; JOICE RODRIGUES DOS SANTOS, Instituto Butantan; ELIZABETH A. L. MARTINS, Instituto Butantan; MARCELO PORTO BEMQUERER, CNPGL; ELISABETH CHENG, Instituto Butantan. |
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Título: |
Non-cryoprecipitation separation of coagulation FVIII and prothrombin complex proteins by pseudoaffinity calcium elution chromatography using anion exchange resin. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Pharmaceuticals, v. 15, n. 10, 1192, 2022. |
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DOI: |
https://doi.org/10.3390/ph15101192 |
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Idioma: |
Inglês |
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Conteúdo: |
Hemophilia A is treated with human plasma coagulation factor VIII (FVIII) replacement therapy and Hemophilia B with coagulation factor IX, which is purified from prothrombin complex concentrate (PCC). In this paper we evaluated the separation of FVIII and PCC by directly loading raw thawed plasma to an anion exchange resin (AEX). Under this relatively high ionic strength, most of the plasma proteins such as albumin, immunoglobulins and others were not adsorbed. Five resins commonly used in protein purification (plasma fractionation) were tested. With all resins, PCC was eluted by pseudoaffinity in a calcium gradient step. Afterwards, FVIII could be recovered with a good yield and high purification factor in the salt gradient step with 400?500 mM NaCl. Using ANX Sepharose FF and Q Sepharose FF, the CaCl2 elution step was introduced after the intermediate wash with 200 mM NaCl, whereas using DEAE Sepharose FF, Fractogel EMD TMAE and Fractogel EMD DEAD, PCC eluted after the wash of the unbound proteins. Our results indicate that three important fractions: (1) albumin, immunoglobulin etc.; (2) PCC; and (3) FVIII can be separated in one chromatographic AEX column and the delicate and troublesome cryoprecipitation can be eliminated, making the purification of blood products faster and cheaper. |
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Palavras-Chave: |
Crioprecipitação; Protrombina; Troca aniônica. |
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Thesagro: |
Análise Química; Coagulação; Cromatografia. |
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Categoria do assunto: |
W Química e Física |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1148380/1/Non-Cryoprecipitation-Separation-of-Coagulation.pdf
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Marc: |
LEADER 02194naa a2200277 a 4500
001 2148380
005 2022-12-01
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.3390/ph15101192$2DOI
100 1 $aFELICIANO, G. P.
245 $aNon-cryoprecipitation separation of coagulation FVIII and prothrombin complex proteins by pseudoaffinity calcium elution chromatography using anion exchange resin.$h[electronic resource]
260 $c2022
520 $aHemophilia A is treated with human plasma coagulation factor VIII (FVIII) replacement therapy and Hemophilia B with coagulation factor IX, which is purified from prothrombin complex concentrate (PCC). In this paper we evaluated the separation of FVIII and PCC by directly loading raw thawed plasma to an anion exchange resin (AEX). Under this relatively high ionic strength, most of the plasma proteins such as albumin, immunoglobulins and others were not adsorbed. Five resins commonly used in protein purification (plasma fractionation) were tested. With all resins, PCC was eluted by pseudoaffinity in a calcium gradient step. Afterwards, FVIII could be recovered with a good yield and high purification factor in the salt gradient step with 400?500 mM NaCl. Using ANX Sepharose FF and Q Sepharose FF, the CaCl2 elution step was introduced after the intermediate wash with 200 mM NaCl, whereas using DEAE Sepharose FF, Fractogel EMD TMAE and Fractogel EMD DEAD, PCC eluted after the wash of the unbound proteins. Our results indicate that three important fractions: (1) albumin, immunoglobulin etc.; (2) PCC; and (3) FVIII can be separated in one chromatographic AEX column and the delicate and troublesome cryoprecipitation can be eliminated, making the purification of blood products faster and cheaper.
650 $aAnálise Química
650 $aCoagulação
650 $aCromatografia
653 $aCrioprecipitação
653 $aProtrombina
653 $aTroca aniônica
700 1 $aARIMORI, S. H.
700 1 $aNAKAO, V. W.
700 1 $aSANTOS, J. R. dos
700 1 $aMARTINS, E. A. L.
700 1 $aBEMQUERER, M. P.
700 1 $aCHENG, M.
773 $tPharmaceuticals$gv. 15, n. 10, 1192, 2022.
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Registro original: |
Embrapa Gado de Leite (CNPGL) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Suínos e Aves. Para informações adicionais entre em contato com cnpsa.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Suínos e Aves. |
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Data corrente: |
13/03/2008 |
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Data da última atualização: |
17/03/2008 |
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Tipo da produção científica: |
Artigo de Divulgação na Mídia |
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Autoria: |
TALAMINI, D. J. D.; MARTINS, F. M.; SOUZA, M. V. N. de. |
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Título: |
Desempenho da avicultura brasileira e mundial em anos recentes. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Avicultura Industrial, v. 99, n. 1162, p. 18-22, 2007. Anuário. |
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Idioma: |
Português |
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Notas: |
Projeto n. 16.00.30001-16. |
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Palavras-Chave: |
Desempenho mundial. |
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Thesagro: |
Avicultura. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00510naa a2200169 a 4500
001 1434908
005 2008-03-17
008 2007 bl --- 0-- u #d
100 1 $aTALAMINI, D. J. D.
245 $aDesempenho da avicultura brasileira e mundial em anos recentes.
260 $c2007
500 $aProjeto n. 16.00.30001-16.
650 $aAvicultura
653 $aDesempenho mundial
700 1 $aMARTINS, F. M.
700 1 $aSOUZA, M. V. N. de
773 $tAvicultura Industrial$gv. 99, n. 1162, p. 18-22, 2007. Anuário.
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Embrapa Suínos e Aves (CNPSA) |
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