Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/10399

TitleSeparation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system
Author(s)Sousa, A.
Passarinha, L. A.
Rodrigues, L. R.
Teixeira, J. A.
Mendonça, A.
Queiroz, J. A.
KeywordsProteose peptone 3
Hydrophobic adsorbents
Dual salt system
Issue dateMay-2008
PublisherJohn Wiley and Sons
JournalBiomedical Chromatography
Citation"Biomedical Chromatography". ISSN 0269-3879. 22:5 (May 2008) 447-449.
Abstract(s)A panel of four hydrophobic adsorbents (butyl-, octyl-, phenyl- and epoxy-Sepharose) was used to examine the selectivity and fractionation of several proteose peptone 3 (PP3) forms from a freeze-dried extract of whey bovine milk. In particular, the effects of altering the ligand type and salt were investigated. The chromatographic studies suggest that PP3 strongly interacts among the three commercial hydrophobic resins leading to a drop off in selectivity, while a complete binding was achieved at low salt concentrations (below 0.5 M) and total elution only with phosphate buffer and/or water stepwise conditions. Only in epoxy–Sepharose was an appreciably selectivity of the several fractions of PP3 present in the initial feedstock attained. Despite the high salt concentration for a complete binding of PP3 (above 1.5 M ammonium sulfate) onto this support, the dual salt system (ammonium sulfate 1 M and sodium citrate 0.8 M) led to a high separation degree of high and low molecular weight forms of PP3.
TypeArticle
URIhttp://hdl.handle.net/1822/10399
DOI10.1002/bmc.961
ISSN0269-3879
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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