[The characteristics of protein hydrolysis on the digestive-transport surfaces of the cestode Eubothrium rugosum and of the intestines of its host--the burbot].

The functioning of different proteinases hydrolysing proteins in a wide pH range, most of which display activity in the alkaline zone of pH, on the digestive-absorptive surfaces of the parasite and host has been investigated. The dynamics of desorption of these proteinases from the intestine of fishes and tegument of cestodes has been studied. It has been shown that the worms possess less proteolytic activity and less capacity for adsorption of proteinases as compared to the intestines of their hosts. The dependence of proteolytic activity of desorbed fractions on the incubation medium temperature has been noted: with the increase in temperature the enzymes, bound closely with the membranes, increase their capacity to hydrolyse proteins. The predominance in cestodes, as compared to the intestine, of easily desorbed fractions D1 and D2 (in the percent ratio of the total proteolytic activity of all fractions) has been detected.