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Hydrophilic interaction chromatography (or hydrophilic interaction liquid chromatography, HILIC) [1] is a variant of normal phase liquid chromatography that partly overlaps with other chromatographic applications such as ion chromatography and reversed phase liquid chromatography. HILIC uses hydrophilic stationary phases with reversed-phase ...
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N-Acetyltaurine can be quantified by a combination of high performance liquid chromatography and mass spectrometry (MS/MS). Due to the high hydrophilicity of N-acetyltaurine, the hydrophilic interaction chromatography (HILIC) is the method of choice in order to separate the analyte from the matrix components. [3] [4]
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Just as in hydrophilic interaction chromatography (HILIC; a sub-technique within HPLC), this method separates analytes based on differences in their polarity. HILIC most often uses a bonded polar stationary phase and a mobile phase made primarily of acetonitrile with water as the strong component. Partition HPLC has been used historically on ...
In 1986, Regnier’s group synthesized a stationary phase that had characteristics of anion exchange chromatography (AEX) and hydrophobic interaction chromatography (HIC) on protein separation. [ 8 ] In 1998, a new form of MMC, hydrophobic charge induction chromatography (HCIC), was proposed by Burton and Harding.
This property distinguishes it from a pure HILIC (hydrophilic interaction chromatography) columns where separation by polar differences is obtained through partitioning into a water-rich layer on the surface, or a pure RP stationary phase on which separation by nonpolar differences in solutes is obtained with very limited secondary mechanisms ...
Pliska and his coworkers [27] used thin layer chromatography to relate mobility values of free amino acids to their hydrophobicities. About a decade ago, another hydrophilicity scale was published, this scale used normal phase liquid chromatography and showed the retention of 121 peptides on an amide-80 column. [ 28 ]