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Biotecnologia Aplicada
Elfos Scientiae
ISSN: 0684-4551
Vol. 14, No. 3, 1997, pp. 189-192
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Bioline Code: ba97043
Full paper language: English
Document type: Research Article
Document available free of charge
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Biotecnologia Aplicada, Vol. 14, No. 3, 1997, pp. 189-192
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Bouyon, Rebeca; Hernandez, Jose R.; Aleaga, Tania; Santana, Hector; Gil, Miriela; Sosa, Raudel; Cruz, Yai; Agraz, Alberto & Herrera, Luis
Resumen
Se realizo un estudio comparativo entre el gel de intercambio cationico de alta resolucion Mono S y los geles de media/alta resolucion TSK SP-650 (S) y SP-Sepharose HP en la purificacion del interferon alpha 2b humano recombinante (rec hu-alpha 2b IFN). La proteina fue eluida de los 3 geles evaluados mediante un gradiente lineal o un gradiente escalonado a 0,1 - 0,19 M de NaCl aproximadamente con un 55 % de recobrado y una pureza superior al 98 %. Con los geles de media/alta resolucion se obtuvo una mayor capacidad de carga (50 mg/mL de gel) que el obtenido con la columna Mono S (10 mg/mL de gel) asi como un aumento en la productividad y la reduccion del costo de la etapa en 2 500 - 3 000 veces. Los geles Fractogel TSK SP-650 y SP-Sepharose HP pueden sustituir al gel de alta resolucion Mono S en la purificacion cromatografica final del rec hu-alpha 2b IFN.
Palabras-clave
cromatografia, interferon alpha 2b humano recombinante, IFN
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Ion exchange chromatography for the purification of recombinant human alpha-2b interferon. Comparative study of medium and high resolution gels
Bouyon, Rebeca; Hernandez, Jose R.; Aleaga, Tania; Santana, Hector; Gil, Miriela; Sosa, Raudel; Cruz, Yai; Agraz, Alberto & Herrera, Luis
Abstract
A comparative study was made of Mono S HR gel, and medium/high resolution Fractogel TSK SP-650 (S) and SP-Sepharose High Performance (SP-Sepharose HP) cationic exchangers for the purification of recombinant human alpha 2b interferon (rec hu-alpha 2b IFN). The protein was eluted through a linear gradient or by stepwise elution with approximately 0.1 - 0.19 M of NaCl. For the 3 gels a 55 % recovery with more than 98 % purity was obtained. The medium/high resolution gels showed higher protein loading capacity (50 mg/mL of gel) than the Mono S column (10 mg/mL of gel), and the productivity was increased. The purification step cost was reduced about 2,500 - 3,000 fold. Fractogel TSK SP-650 and SP-Sepharose HP can substitute high resolution Mono S for the final chromatographic purification of rec hu-alpha 2b IFN.
Keywords
chromatography, recombinant human alpha 2b interferon, IFN
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© Copyright 1997 Elfos Scientiae Alternative site location: http://elfosscientiae.cigb.edu.cu/Archivo.asp?Id=6
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