background: among diverse protein purification systems, affinity chromatography is the most attractive one in the purification process of coagulation factors. coagulation factor vii is a plasma serine protease that has a significant role in natural human hemostasis and its recombinant form such as aryoseventm, has been applied in clinical treatment of bleeding disorders. immunoaffinity chromato...

functional resemblance of column groups to carbamoyl phosphate. The enzyme binds its two substrates, carbamoyl phosphate and L-aspartate, in an obligatory order, with carbamoyl phosphate leading (Grayson et al., 1979). If column groups are sufficiently similar to carbamoyl phosphate, the enzyme should be adsorbed more tightly in the presence of L-aspartate, owing to the ‘locking-on’ effect (O’C...

Affinity chromatography is a type of liquid chromatography that makes use of biological-like interactions for the separation and specific analysis of sample components. This review describes the basic principles of affinity chromatography and examines its use in the testing of clinical samples, with an emphasis on HPLC-based methods. Some traditional applications of this approach include the us...

The glycine receptor of rat spinal cord was solubilized with the nonionic detergent Triton X-100 and subsequently purified by affinity chromatography on aminostrychnine-agarose and wheat germ agglutininSepharose. An overall purification of 1950-fold was achieved. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethano1 revealed three glycine receptor-asso...

A simple method for the purification of staphylococcal enterotoxins A (SEA), B (SEB), and C2 (SEC2) from fermentor-grown cultures was developed. The toxins were purified by pseudo-affinity chromatography by using the triazine textile dye "Red A" and gave overall yields of 49% (SEA), 44% (SEB), and 53% (SEC2). The purified toxins were homogeneous when analyzed by sodium dodecyl sulfate-polyacryl...

Affinity chromatography is a technique used to purify compounds, such as proteins, that have the ability to non-covalently and reversibly bind specific molecules, known as ligands. This method differs from the classical chromatography techniques in that the protein is purified on the basis of a unique biochemical property. In affinity chromatography, the ligand is covalently attached to a matri...