Abstract
Abstract A variety of proteins adsorbed to Sephacryl gels, S-200, S-500 and S-1000 and Fractogel TSK-HW65(F) in the presence of high concentrations of ammonium sulfate. The adsorption of these proteins to individual gel matrices showed some variations. The strength of adscrption. of cytochrome c, myoglobin and chymotrypsinogen A to Sephacryl S-200 increased with temperature and pH, suggesting that hydrophobic interaction is involved in the adsorption. The chromatographic behaviour of these three proteins on Sephacryl S-type gels and Fractogel varied with the ammonium sulfate concentration of the eluant buffer. At 30% saturation, cytochrome c and myoglobin eluted together and followed by chymotrypsinogen A. At 45% saturation, however cytochrome c eluted before myoglobin and chymotrypsinogen A remained tightly bound to the column. Temperature, pH, flow-rate and glycerol were some of the factors affecting the separation of these three proteins on Sephacryl S-200.
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