[Study of conformational changes in alcohol dehydrogenase during its interaction with silochrome adsorbent by the EPR spectroscopy method].

The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.