Journal of Biochemistry Research

Affinity Chromatography Quality Articles

Affinity chromatography may be a method of separating biochemical mixture supported a highly specific interaction between antigen and antibody, enzyme and substrate, receptor and ligand, or protein and macromolecule. It's a kind of chromatographic laboratory technique used for purifying biological molecules within a mix by exploiting molecular properties, e.g. protein are often eluted by ligand solution. Biological macromolecules, like enzymes and other proteins, interact with other molecules with high specificity through several differing types of bonds and interaction. Such interactions include hydrogen bonding, ionic interaction, disulfide bridges, hydrophobic interaction, and more. The high selectivity of Affinity chromatography is caused by allowing the specified molecule to interact with the stationary phase and be bound with in the column so as to be separated from the undesired material which can not interact and elute first. The molecules not needed are first washed away with a buffer while the specified proteins are abandoning within the presence of the eluting solvent (of higher salt concentration). This process creates a competitive interaction between the specified protein and therefore the immobilized stationary molecules, which eventually lets the now highly purified proteins be released. Affinity chromatography are often wont to purify and concentrate a substance from a mix into a buffering solution, reduce the quantity of unwanted substances during a mixture, identify the biological compounds binding to a specific substance, purify and concentrate an enzyme solution. The molecule of interest are often immobilized through covalent bonds.

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