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1 2003

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Wykorzystanie chromatografii z unieruchomionym jonem metalu do izolowania białek

Wójcik M., Koziołkiewicz M.

Wiadomości Chemiczne

2003

[Z] 57, 1-2

99--113

Immobilized metal affinity chromatography (IMAC) is a widely used technique for separation of proteins with natural surface-exposed histidine residues and recombinant proteins with polyhistidine fusion tags in particular [1-7]. IMAC is a type of an affinity chromatography which gives an opportunity to separate proteins based on the binding of proteins to transition metals. This occurs via the electron-donating side chain of residues such as histidine and cysteine, which substitute water molecules coordinated to the metal. Due to the fact that metal affinity is sensitive to the exposure and spatial arrangement of histidine residues, IMAC can probe structural changes expressed on protein surfaces as a result of partial digestion, unfolding, or association with other molecules [8]. Overall, IMAC is a quick method which limits the number of procedures in the process of puryfing proteins thereby reducing the cost of their isolation. This paper describes influence of the type and the number of electro-donor surface groups, the type of metal immobilized with the stationary phase and pH of the mobile phase on the selectivity of an affinity separation.