Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/107238
Type: Artigo de periódico
Title: Partitioning Of Whey Proteins, Bovine Serum Albumin And Porcine Insulin In Aqueous Two-phase Systems
Author: Alves J.G.L.F.
Chumpitaz L.D.A.
Da Silva L.H.M.
Franco T.T.
Meirelles A.J.A.
Abstract: Partitioning 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.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/S0378-4347(00)00111-0
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0034705829&partnerID=40&md5=870c21c4f7f6fb5aa50c400682fa1ee2
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

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