[Sorption immobilization of NAD-dependent enzyme systems. I. Influence of electrostatic interactions on the orientation of alcohol dehydrogenase on the sorbent surface].
The model calculation of interactions between the horse liver alcoholdehydrogenase-globule and the charged surface of sorbents and electrodes was performed. It has been shown that due to the discrete distribution of charges the enzyme globula can sorb on the surfaces having the same sign of charge as the total globule charge. In case of alcoholdehydrogenase the anion sorption can occur at pH greater than pI. Also, the orientation and therefore the catalytic activity of the immobilized system can be optimal.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D004563:Electrochemistry; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006736:Horses; D008099:Liver / Q000201:enzymology; D009243:NAD; D011485:Protein Binding
D004800:Enzymes, Immobilized; D009243:NAD; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase
Sorbtsionnaia immobilizatsiia NAD-zavisimykh fermentativnykh sistem. I. Vliianie élektrostaticheskikh vzaimodeĭstviĭ na orientatsiiu alkogol'degidrogenazy na poverkhnosti nositelia.