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Increased Antiviral Activity of Microscale-Purified HuIFN Alpha 8 (Human Interferon Alpha 8) Over HuIFN Alpha 2b in Hep-2 Cells Challenged With Mengo Virus

Julio César Sánchez García, Alejandro Miranda Ariza, Alexis Musacchio Lasa, Luis Javier González, Vladimir Besada Perez

Biotechnol Appl Biochem. 2007 Nov;48(Pt 3):159-65.

PMID: 17523917

Abstract:

Human proteins are not routinely expressed at high levels in Escherichia coli for, among other reasons, different codon usage. Several purification procedures have been applied to recover recombinant proteins for further biological characterization. However, the vast majority involve costly chromatography procedures. In the present study, both (Hu)IFN(alpha 2b) (human interferon alpha 2b) and (Hu)IFN(alpha 8) were expressed efficiently in E. coli BL21-codonplus-RIL. Subsequently, both recombinant proteins were purified to homogeneity by passive elution from reverse-stained SDS/PAGE gels, a cost-effective purification procedure. After purification, both recovered proteins were biologically active. The (Hu)IFN(alpha 8) subtype induced 1.46-fold more antiviral activity than (Hu)IFN(alpha 2b) using Hep-2 human laryngeal carcinoma cell challenged with Mengo virus.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR4248761 IFN-alpha 2b human IFN-alpha 2b human Price
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