dc.creatorVancan, S
dc.creatorMiranda, EA
dc.creatorBueno, SMA
dc.date2002
dc.date40179
dc.date2014-11-14T17:20:03Z
dc.date2015-11-26T16:07:41Z
dc.date2014-11-14T17:20:03Z
dc.date2015-11-26T16:07:41Z
dc.date.accessioned2018-03-28T22:56:21Z
dc.date.available2018-03-28T22:56:21Z
dc.identifierProcess Biochemistry. Elsevier Sci Ltd, v. 37, n. 6, n. 573, n. 579, 2002.
dc.identifier1359-5113
dc.identifierWOS:000173977500002
dc.identifier10.1016/S0032-9592(01)00242-4
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/69221
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/69221
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/69221
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1266193
dc.descriptionHuman IgG is an important plasma protein produced worldwide on a large scale. Affinity chromatographic processes are not commercially used for the production of IgG since the ligands tried so far hinder their application to pharmaceutical products. Immobilized ion affinity chromatography (IMAC) has the potential to circumvent these problems. The adsorption of human IgG onto IDA-Sepharose immobilized Cu2+, Ni2+, Zn2+, and Co2+ with MOPS, phosphate, MMA, and Tris-HCI adsorption buffering systems is reported. Adsorption of high purity IgG was high for all metals irrespective of the buffer system used. Elution of IgG was similar for all buffer systems except for the case of pH elution when copper was the ligand. Isoeletrocfocusing showed the presence of molecules of low pI in the flowthrough of the chromatographic runs with Ni2+-phosphate-acetate, Ni2+-MOPS-imidazole and Zn2+-MOPS-imidazole systems. Chromatography runs with human plasma indicated the potential of this technique for IgG purification. (C) 2002 Elsevier Science Ltd. All rights reserved.
dc.description37
dc.description6
dc.description573
dc.description579
dc.languageen
dc.publisherElsevier Sci Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationProcess Biochemistry
dc.relationProcess Biochem.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectIMAC
dc.subjectIgG
dc.subjectpurification
dc.subjecthuman plasma
dc.subjectchromatography
dc.subjectaffinity
dc.subjectMetal-affinity-chromatography
dc.subjectOne-step Purification
dc.subjectImmunoglobulin-g
dc.subjectHuman Plasma
dc.subjectProtein
dc.subjectFractionation
dc.subjectAdsorption
dc.subjectBinding
dc.titleIMAC of human IgG: studies with IDA-immobilized copper, nickel, zinc, and cobalt ions and different buffer systems
dc.typeArtículos de revistas


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