Denatured Thermodynamics of Proteins in Weak Cation-exchange Chromatography

来源 :Chemical Research in Chinese Universities | 被引量 : 0次 | 上传用户:wplyaq
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The thermostability of some proteins in weak cation-exchange chromatography was investigated at 20-80 ℃. The results show that there is a fixed thermal denaturation transition temperature for each protein. The appearance of the thermal transition temperature indicates that the conformations of the proteins are destroyed seriously. The thermal behavior of the proteins in weak cation-exchange and hydrophobic interaction chromatographies were compared in a wide temperature range. It was found that the proteins have a higher thermostability in a weak cation-exchange chromatography system. The thermodynamic parameters(Δ H 0, Δ S 0) of those proteins were determined by means of Vant Hoff relationship(ln k -1/ T ). According to standard entropy change(Δ S 0), the conformational change of the proteins was judged in the chromatographic process. The linear relationships between Δ H 0 and Δ S 0 can be used to evaluate “compensation temperature”( β ) at the protein denaturation and identify the identity of the protein retention mechanism in weak cation-exchange chromatography. The thermostability of some proteins in weak cation-exchange chromatography was investigated at 20-80 ° C. The results show that there is a fixed thermal denaturation transition temperature for each protein. The appearance of the thermal transition temperature indicates that the conformations of the proteins are The thermal behavior of the proteins in weak cation-exchange and hydrophobic interaction chromatographies were compared in a wide temperature range. It was found that the proteins have a higher thermostability in a weak cation-exchange chromatography system. The thermodynamic parameters (Δ H 0, Δ S 0) of those proteins were determined by means of Vant Hoff relationship (ln k -1 / T). According to standard entropy change (Δ S 0), the conformational change of the proteins was judged in The chromatographic process. The linear relationships between ΔH 0 and ΔS 0 can be used to evaluate “compensation temperature” (β) at th e protein denaturation and identify the identity of the protein retention mechanism in weak cation-exchange chromatography.
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