Enzyme purification by hydrophobic chromatography: an alternative approach illustrated in the purification of aspartate transcarbamoylase from wheat germ.
Two adsorbents containing similar numbers of hydrocarbon (C(10)) chains but different numbers of carboxyl groups were made by chemical modification of Sepharose. The use of these adsorbents to purify proteins, under conditions where hydrophobic adsorption is partly resisted by electrostatic repulsion, is illustrated in the purification of aspartate transcarbamoylase (EC 2.1.3.2) from wheat germ.
D000327:Adsorption; D001221:Aspartate Carbamoyltransferase / Q000302:isolation & purification*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D005069:Evaluation Studies as Topic; D006882:Hydroxyapatites; D008722:Methods; D010944:Plants / Q000201:enzymology*; D011134:Polysaccharides; D013056:Spectrophotometry, Ultraviolet; D014908:Triticum / Q000201:enzymology
D006882:Hydroxyapatites; D011134:Polysaccharides; D001221:Aspartate Carbamoyltransferase