The interaction between the metal chelate ligand and proteins and the selectivity of metal chelate chromatography can be changed through changing chromatographic conditions.

改变色谱条件可改变金属螯合配体和蛋白质间的作用力，提高金属螯合色谱的选择性。

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The interaction between chelating weak cation-exchanger and metal ions was examined. The retention mechanism of protein in metal chelating chromatography was explored.

考察了螯合型弱阳离子交换剂与金属离子的作用，研究了蛋白质在金属螯合色谱中的保留机理。

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By immobilized metal affinity chromatography, ion-exchange chromatography and hydrophobic interaction chromatography, the recombinant Gln49-PLA2 was purified with 91% purity.

通过固定化金属亲和层析、阴离子交换、疏水层析融合蛋白得到了纯化，其纯度可达91%。

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