dc.creatorAlves J.G.L.F.
dc.creatorChumpitaz L.D.A.
dc.creatorDa Silva L.H.M.
dc.creatorFranco T.T.
dc.creatorMeirelles A.J.A.
dc.date2000
dc.date2015-06-30T19:50:39Z
dc.date2015-11-26T14:47:09Z
dc.date2015-06-30T19:50:39Z
dc.date2015-11-26T14:47:09Z
dc.date.accessioned2018-03-28T21:57:20Z
dc.date.available2018-03-28T21:57:20Z
dc.identifier
dc.identifierJournal Of Chromatography B: Biomedical Sciences And Applications. , v. 743, n. 01/02/15, p. 235 - 239, 2000.
dc.identifier13872273
dc.identifier10.1016/S0378-4347(00)00111-0
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0034705829&partnerID=40&md5=870c21c4f7f6fb5aa50c400682fa1ee2
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/107238
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/107238
dc.identifier2-s2.0-0034705829
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1253147
dc.descriptionPartitioning of the proteins from cheese whey, bovine serum albumin and porcine insulin were analysed using aqueous two-phase systems (ATPS) prepared with PEG-phosphate, PEG-citrate and PEG-maltodextrin (MD). Proteins were quantified through one of the following methods: FPLC, Bradford and spectrophotometry at 280 nm. Results showed that whey proteins partitioned unevenly on the phases of the systems used, with α-lactoalbumin (α-La) concentrated in the upper phase and β-lactoglobulin (β-Lg) in the lower. Albumin in PEG-MD systems concentrated in the MD-rich lower phase. Porcine insulin showed great affinity with the PEG-rich phase, its partition coefficient was always over 10 and increases with PEG molecular mass. (C) 2000 Elsevier Science B.V.
dc.description743
dc.description01/02/15
dc.description235
dc.description239
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dc.languageen
dc.publisher
dc.relationJournal of Chromatography B: Biomedical Sciences and Applications
dc.rightsfechado
dc.sourceScopus
dc.titlePartitioning Of Whey Proteins, Bovine Serum Albumin And Porcine Insulin In Aqueous Two-phase Systems
dc.typeArtículos de revistas


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