Adsorption chromatography on Toyopearl: a single-step alternative to salt fractionation of protein mixtures.
Toyopearl media for gel filtration tend to adsorb proteins at high ionic strength, presumably by hydrogen bonding. This is used in the technique proposed here for resolution of crude protein mixtures and initial purification of their components. Proteins can be selectively adsorbed on a column of Toyopearl at high ammonium sulfate concentration and then eluted by decreasing the salt concentration. This single-step procedure can replace the usual salt fractionation of protein mixtures, which is demonstrated with yeast cytochrome oxidase.
D000327:Adsorption; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003576:Electron Transport Complex IV / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D008928:Mitochondria / Q000201:enzymology; D011108:Polymers; D011506:Proteins / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013053:Spectrophotometry; D013367:Submitochondrial Particles / Q000201:enzymology
D011108:Polymers; D011506:Proteins; C044554:Toyopearl HW-65F; D003576:Electron Transport Complex IV