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HPLC has many applications in both laboratory and clinical science. It is a common technique used in pharmaceutical development, as it is a dependable way to obtain and ensure product purity. [59] While HPLC can produce extremely high quality (pure) products, it is not always the primary method used in the production of bulk drug materials. [60]
Subtle differences in a compound's partition coefficient result in differential retention on the stationary phase and thus affect the separation. [1] Chromatography may be preparative or analytical. The purpose of preparative chromatography is to separate the components of a mixture for later use, and is thus a form of purification.
Fast protein liquid chromatography (FPLC) is a form of liquid chromatography that is often used to analyze or purify mixtures of proteins. As in other forms of chromatography, separation is possible because the different components of a mixture have different affinities for two materials, a moving fluid (the mobile phase) and a porous solid (the stationary phase).
The basic methods of separation in HPLC rely on a mobile phase (water, organic solvents, etc.) being passed through a stationary phase (particulate silica packings, monoliths, etc.) in a closed environment (column); the differences in reactivity among the solvent of interest and the mobile and stationary phases distinguish compounds from one ...
Silica gel particles are commonly used as a stationary phase in high-performance liquid chromatography (HPLC) for several reasons, [13] [14] including: High surface area: Silica gel particles have a high surface area, allowing direct interactions with solutes or after bonding of variety of ligands for versatile interactions with the sample molecules, leading to better separations.
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.
Likewise, differences between conformation of the analyte and the standard have no effect on an absolute measurement; for example, with MALS analysis, the molar mass of inherently disordered proteins are characterized accurately even though they elute at much earlier times than globular proteins with the same molar mass, and the same is true of ...
As in any chromatography, equilibrium is established between molecules of a given kind bound to the matrix and those of the same kind free in solution. Because the number of binding sites is finite, when the concentration of molecules free in solution is large relative to the dissociation constant for the sites, those sites will mostly be filled.