Differential salt-promoted chromatography for protein purification.
A range of hydrophobic-type adsorbents for protein chromatography has been screened for the binding, at high salt concentrations, of 10 enzymes from a bacterial extract. Adsorbents were chosen for tandem chromatography, in which the first adsorbent removed much of the protein, and the second and subsequent columns bound the desired enzymes. Simple schemes for isolating Zymomonas mobilis and yeast alcohol dehydrogenases are described, in which the enzymes are affinity eluted by NAD+.
Scopes
R K
RK
Centre for Protein and Enzyme Technology, La Trobe University, Bundoora, Victoria, Australia.
Porath
J
J
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification*; D002845:Chromatography / Q000379:methods*; D006092:Gram-Negative Facultatively Anaerobic Rods / Q000201:enzymology*; D012492:Salts
D012492:Salts; D000426:Alcohol Dehydrogenase