[Sorption immobilization of NAD-dependent enzyme systems. II. Influence of hydrophobic interactions on the orientation of alcohol dehydrogenase on the sorbent surface].
The model calculation of hydrophobic interactions between the horse liver alcoholdehydrogenase globule and the uncharged surface of the hydrophobic sorbent was performed. The most probable orientation of the globula on the surface was found. It has been shown that the immobilized system with this orientation has the maximum catalytic activity.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006736:Horses; D008099:Liver / Q000201:enzymology; D008958:Models, Molecular; D009243:NAD; D011485:Protein Binding; D011487:Protein Conformation
D004800:Enzymes, Immobilized; D009243:NAD; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase
Sorbtsionnaia immobilizatsiia NAD-zavisimykh fermentnykh sistem. II. Vliianie gidrofovnykh vzaimodeĭstviĭ na orientatsiiu alkogol'degidrogenazy na poverkhnosti nositelia.