Gel-filtration chromatography is a versatile method that permits the effective separation of biological molecules in high yield. This article describes the basis of the method, the selection of suitable operating conditions, and contrasts typical matrix types. Applications of the technique are described, with references to the scientific literature.

the aim of the present work was to purify cysteine protease inhibitors from rapeseed (brassica napus l.), with potential activity on digestive protease of colorado potato beetle (cpb), leptinotarsa decemlineata (say). ammonium sulfate precipitated proteinaceous fractions; 30, 50, 70, and 100% showed 39.07, 57.03, 51.47, and 22.44% inhibition on the fourth instar larval gut general protease acti...

We have developed a facile means for the refolding of milligram quantities of purified proteins that employs gel filtration chromatography. We demonstrate by electrophoretic mobility shift and NMR spectroscopy that human ETS-1 protein, bovine ribonuclease A and E. coli integration host factor can be refolded into the native conformation using this technique. We have extended this strategy to th...

A procedure is described for purifying a low molecular weight peptide that induces differentiation in mouse myeloid leukemia M1 cells. The factor comes from the conditioned medium of macrophage-like cells differentiated from mouse myeloid leukemia M1 cells. The procedure for purification includes gel filtration on Sephadex G-15, anionic exchange chromatography, thin-layer chromatography, revers...

Tonin has been purified from rat submaxillary glands. The purification procedure included affinity chromatography on Sepharose 4B coupled to antitonin followed by DEAE chromatography and gel filtration on Sephadex G-100. Homogeneity of the purified enzyme was confirmed by Sephadex G-100 gel filtration, disc electrophoresis, and isoelectric focusing on polyacrylamide gel, immunodiffusion, and im...

A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was u...

The extracellular endo-1,4-beta-glucanase components of Ruminococcus flavefaciens FD-1 were analyzed by high-performance liquid chromatography (HPLC) by using DEAE ion-exchange, hydroxylapatite, and gel filtration chromatography and polyacrylamide gel electrophoresis (PAGE). Two endo-1,4-beta-glucanase peaks were resolved by DEAE-HPLC and termed endoglucanases A and B. Carboxymethyl cellulose (...