Expression of glycosylated proteins in bacterial system and purification by affinity chromatography

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.contributorUniversidade de São Paulo (USP)
dc.date.accessioned2022-04-29T08:14:25Z
dc.date.accessioned2022-12-20T02:38:20Z
dc.date.available2022-04-29T08:14:25Z
dc.date.available2022-12-20T02:38:20Z
dc.date.created2022-04-29T08:14:25Z
dc.date.issued2018-01-01
dc.identifierMethods in Molecular Biology, v. 1674, p. 183-191.
dc.identifier1064-3745
dc.identifierhttp://hdl.handle.net/11449/228390
dc.identifier10.1007/978-1-4939-7312-5_14
dc.identifier2-s2.0-85029700402
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5408525
dc.description.abstractThe bacterial expression of glycoproteins has experienced significant progress in recent years, particularly in regard to the production of conjugate vaccines against pathogens. In this case, a protein carrier conjugated with glycosides is used to produce intense stimulation of the immune system. Glycoconjugate vaccines account for 35% of the global vaccine market, and consequently, several biotechnological companies have developed products for the purification of glycosylated proteins to attain homogeneity. In this chapter we present a general process for glycoprotein production in Escherichia coli and a practice method for purification of glycosylated proteins, using affinity chromatography.
dc.languageeng
dc.relationMethods in Molecular Biology
dc.sourceScopus
dc.subjectAffinity chromatography
dc.subjectBacterial expression
dc.subjectConjugate vaccines
dc.subjectGlycosylated protein
dc.titleExpression of glycosylated proteins in bacterial system and purification by affinity chromatography
dc.typeCapítulos de libros


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