2007
DOI: 10.1016/j.jbbm.2006.12.001
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Induced binding of proteins by ammonium sulfate in affinity and ion-exchange column chromatography

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Cited by 15 publications
(9 citation statements)
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“…4. Arakawa et al (25) had similar results, since the low ammonium sulfate concentration was the most successful condition to elute BSA, considering its molarities under evaluation.…”
Section: Resultsmentioning
confidence: 74%
“…4. Arakawa et al (25) had similar results, since the low ammonium sulfate concentration was the most successful condition to elute BSA, considering its molarities under evaluation.…”
Section: Resultsmentioning
confidence: 74%
“…The supernatant was diluted into 2 M ammonium sulfate containing binding buffer for a modified Blue-Sepharose chromatography, described previously (23) and eluted using 2 M NaCl (Eluate 1) and 1 M arginine (Eluate 2). The eluted fractions were concentrated and dialyzed against phosphate-buffered saline (PBS) using Vivaspin 6 columns (GE Healthcare) and then tested for induction of TEAD activity using luciferase assay (described below).…”
Section: Methodsmentioning
confidence: 99%
“…All these results are consistent with hydrophobic binding to the highly hydrophilic resin in the presence of salting‐out salts. In fact, ammonium sulfate even produces binding of proteins to highly polar ion exchange columns, which simply reflects its strong salting‐out property 49, 50…”
Section: Solvent Effectsmentioning
confidence: 99%