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Mendeley readers
Chapter title |
Purification Method for Recombinant hG-CSF by Affinity Chromatography
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Chapter number | 16 |
Book title |
Recombinant Glycoprotein Production
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Published in |
Methods in molecular biology, January 2018
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DOI | 10.1007/978-1-4939-7312-5_16 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7311-8, 978-1-4939-7312-5
|
Authors |
Bruna Samham Archangelo, Elisa Maria de Sousa Russo |
Abstract |
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. |
Mendeley readers
The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 2 | 40% |
Professor | 1 | 20% |
Student > Bachelor | 1 | 20% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 1 | 20% |
Agricultural and Biological Sciences | 1 | 20% |
Earth and Planetary Sciences | 1 | 20% |
Engineering | 1 | 20% |
Unknown | 1 | 20% |