2004
DOI: 10.1016/j.jchromb.2004.03.066
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Separation of cobalt binding proteins by immobilized metal affinity chromatography

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Cited by 15 publications
(9 citation statements)
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“…The salting-out ability can also be related to the Gibbs energy of hydration of the ions. Because these salts share a common cation but contain different anions, it is easy to find that the salting-out ability of these anions follows the order: PO 4 3− ( G hyd = −2765 kJ mol −1 ) > CO 3 2− ( G hyd = −1315 kJ mol −1 ) > OH − ( G hyd = −430 kJ mol −1 ) [28]. This order follows the Hofmeister series for the strength of the kosmotropic salts.…”
Section: Phase Diagrammentioning
confidence: 99%
See 1 more Smart Citation
“…The salting-out ability can also be related to the Gibbs energy of hydration of the ions. Because these salts share a common cation but contain different anions, it is easy to find that the salting-out ability of these anions follows the order: PO 4 3− ( G hyd = −2765 kJ mol −1 ) > CO 3 2− ( G hyd = −1315 kJ mol −1 ) > OH − ( G hyd = −430 kJ mol −1 ) [28]. This order follows the Hofmeister series for the strength of the kosmotropic salts.…”
Section: Phase Diagrammentioning
confidence: 99%
“…Traditional methods to purify proteins involve several steps such as ammonium sulfate precipitation, ionic and affinity chromatography [3], or electrophoresis [4]. However, some of these separation techniques are time and cost consuming.…”
Section: Introductionmentioning
confidence: 99%
“…Moreover, when these processes are applied to biological materials, rigorous purification steps, delicate enough to preserve the biological activity, are required. The most common techniques used are the ammonium sulphate precipitation [7], ionic and affinity chromatography [8,9], dialysis, filtration, electrophoresis [10][11][12][13] and reverse micelles approaches [14,15]. Nevertheless, some of these separation processes are costly and time consuming, and are not easily scalable [7].…”
Section: Introductionmentioning
confidence: 99%
“…12 Hence, a large number of IMAC strategies have been developed in the case of pre-fractionate proteins for metalloproteomic investigation by immobilizing different metal ions, 13 such as Zn 2+ , Ni 2+ , Cu 2+ and Co 2+ . [14][15][16] By using chelating Sepharose Fast Flow resin (Amersham Biosciences), She et al 17 analysed Cu and Zn metalloproteomes in three human hepatoma cell lines (Hep G2, Mz-Hep-1 and SKHep-1), and Smith et al 18 identified 67 copper-binding proteins in the cytoplasmic and microsomal fractions of Hep G2 cells. Wang et al 19 carried out a systematic screening for copper-binding proteins in soybean seeds by using IMAC technology.…”
Section: Introductionmentioning
confidence: 99%