The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography

Sattar Al-Jibbouri

doi:10.1016/j.chroma.2006.10.079

The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography

Sattar Al-Jibbouri

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

In this paper, an analysis of the influence of the salt types, NaCl, NaCH"3COO, Na"2SO"4 and Na"3C"6H"5O"7, on the isocratic retention behaviour of bovine serum albumin (BSA) on two anion-exchangers media (Source 30Q and TSK Gel Super Q 5 PW) has been presented. The retention data demonstrated that the mechanism of protein retention in ion-exchange chromatography (IEC) involves interactions between the protein solute, the mobile phase constituents and the stationary phase. The effect of protein activity coefficient in the mobile phase on the protein retention volumes is verified.

Original language	English
Journal	Journal of Chromatography A
Volume	1139
Issue number	1
Pages (from-to)	57-62
ISSN	0021-9673
DOIs	https://doi.org/10.1016/j.chroma.2006.10.079
Publication status	Published - 2007

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title = "The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography",

abstract = "In this paper, an analysis of the influence of the salt types, NaCl, NaCH{"}3COO, Na{"}2SO{"}4 and Na{"}3C{"}6H{"}5O{"}7, on the isocratic retention behaviour of bovine serum albumin (BSA) on two anion-exchangers media (Source 30Q and TSK Gel Super Q 5 PW) has been presented. The retention data demonstrated that the mechanism of protein retention in ion-exchange chromatography (IEC) involves interactions between the protein solute, the mobile phase constituents and the stationary phase. The effect of protein activity coefficient in the mobile phase on the protein retention volumes is verified.",

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AB - In this paper, an analysis of the influence of the salt types, NaCl, NaCH"3COO, Na"2SO"4 and Na"3C"6H"5O"7, on the isocratic retention behaviour of bovine serum albumin (BSA) on two anion-exchangers media (Source 30Q and TSK Gel Super Q 5 PW) has been presented. The retention data demonstrated that the mechanism of protein retention in ion-exchange chromatography (IEC) involves interactions between the protein solute, the mobile phase constituents and the stationary phase. The effect of protein activity coefficient in the mobile phase on the protein retention volumes is verified.

U2 - 10.1016/j.chroma.2006.10.079

DO - 10.1016/j.chroma.2006.10.079

M3 - Journal article

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SP - 57

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JO - Journal of Chromatography A

JF - Journal of Chromatography A

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ER -

The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography

Abstract

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