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M I Goriaev

Publications and source records attributed to M I Goriaev.

6 recordsLinked to original sources

[Effect of naphthenic acids on the permeability of ascitic tumor cells to potassium ions].

Ascite cells were treated with naphthenic acid preparation, containing a mixture of naphthenic acids with average molecular weight equal to 240, and with a fraction of this preparation differing in the boiling temperature. A 5-10(-7)M and higher concentrations of the preparation and its fraction brought about an increased permeability in ascite cells for K-ions. The effectiveness of naphthenic acids is associated with their hydrophobic properties, which was characterized in the present communication by the value of hydrophilic-lipophilic balance calculated according to the Davies formula.

Animals↗

[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.

Alcohol Dehydrogenase↗

[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.

Alcohol Dehydrogenase↗