Publication: Development of fast and simple methods for porcine haptoglobin and ceruloplasmin purification
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Date
2010
Authors
Fuentes, P. ; Gutiérrez Andrés, M. ; Soler, L. ; Cerón Madrigal, José Joaquín ; Martínez Subiela, Silvia
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Facultad de Veterinaria
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Publisher
Murcia, Universidad de Murcia, Servicio de Publicaciones
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Two fast and simple methods for porcine haptoglobin (Hp) and ceruloplasmin (Cp) purification are described in this paper. Hp was purified by ammonium sulphate fractionation and a FPLC Superdex-200 gel chromatography. The protein obtained showed two bands with a Mr (molecular mass) of about 44 kDa and 12.9 kDa corresponding to heavy (ß) and light (a) chains of Hp respectively, on sodium dodecyl sulphate-polyacrilamide gel electrophoresis, under reducing conditions. Ceruloplasmin (Cp) was isolated by one step of chromatography on amino-ethyl-derivatized Sepharose followed by gel filtration on a Superdex-200 column. The Mr of the protein, as estimated by SDS-PAGE was approximately 150 kDa. In conclusion, two new protocols have been developed for porcine Hp and Cp purification, being less time-consuming and technically demanding than those previously reported. This paper could represent an interesting guideline and be of help to obtain pure protein to use as specie-specific standard material and to produce specific antibodies.
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Citation
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