Artículos de revistas
Human interferon B1 ser17: Coding DNA synthesis, expression, purification and characterization of bioactive recombinant protein
Journal of Microbial and Biochemical Technology, v. 2, n. 5, p. 111-117, 2010.
Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
Quatro G Pesquisa e Desenvolvimento LTDA
Universidade Estadual Paulista (Unesp)
Universidade Federal de Santa Maria (UFSM)
A protocol to produce large amounts of bioactive homogeneous human interferon β1 expressed in Escherichia coli was developed. Human interferon β1 ser17 gene was constructed, cloned and subcloned, and the recombinant protein expressed in E. coli cells. Solubilization of recombinant human interferon β1 ser17 (rhIFN-β1 ser17) was accomplished by employing a brief shift to high alkaline pH in the presence of non-ionic detergent. The recombinant protein was purifi ed by three chromatographic steps. N-terminal amino acid sequencing and mass spectrometry analysis provided experimental evidence for the identity of the recombinant protein. Reverse phase liquid chromatography demonstrated that the content of deamidates and sulphoxides was similar to a commercial standard. Size exclusion chromatography demonstrated the absence of high molecular mass aggregates and dimers. The protocol represents an effi cient and high-yield method to obtain bioactive homogeneous monomeric rhIFN-β1 ser17 protein. It may thus represent an important step towards scaling up for rhIFN-β1 ser17 large-scale production. © 2010 Villela AD, et al.
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