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Published on: July 12, 2018
Purification Method for Recombinant hG-CSF by Affinity Chromatography
Bruna Samham Archangelo1, Elisa Maria de Sousa Russo2
1School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil.
The human granulocytic colony-stimulating factor (hG-CSF) acts mainly by promoting the maturation of granulocytes and stimulating their phagocytic and chemotactic activity. It has been used in the treatment of many diseases, in particular in neutropenic conditions. Here, we describe the purification process of the recombinant protein hG-CSF expressed in Pichia pastoris. The protein purification proved to be efficient using the nickel affinity chromatography method described in this chapter.
The human granulocytic colony-stimulating factor (hG-CSF) acts mainly by promoting the maturation of granulocytes and stimulating their phagocytic and chemotactic activity. It has been used in the treatment of many diseases, in particular in neutropenic conditions. Here, we describe the purification process of the recombinant protein hG-CSF expressed in Pichia pastoris. The protein purification proved to be efficient using the nickel affinity chromatography method described in this chapter.

