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- W2010672862 abstract "High-performance separations of proteins, based on immobilized-metal affinity chromatography (HPIMAC), are described. The Stationary phase consisted of imonidiacetic acid (IDA) chelate groups, bonded to samll particle, wide pore silica gel by means of a polyether hydrophilic leash. After loading the column with metal, retention of proteins was achieved by protein—metal complexation at high concentrations of sodium sulfate. Elution was accomplished by addition of competitive complexing ligands, such as ammonia at constant pH, and/or by a decreasing pH gradient of a specially designed buffer system to maintain buffer capacity constant throughout the gradient. Selective separations, based on differences in the number of histidine residues present on the surface of the proteins, are described. The application of HPIMAC in the separation and purification of structurally similar proteins is presented. The potential application of IDA columns in three chromatographic modes (HPIMA, hydrophobic interactions, and cation exchange) is also described." @default.
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- W2010672862 date "1986-12-01" @default.
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- W2010672862 title "High-performance immobilized-metal affinity chromatography of proteins of iminodiacetic acid silica-based bonded phases" @default.
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- W2010672862 doi "https://doi.org/10.1016/s0021-9673(01)94717-x" @default.
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