[Effect of arginine and its analogs on the activity of lysosomal and nonlysosomal peptide hydrolases in rat tissues].

The autolysis intensity and proteolysis activity at pH 4,5, 7,4, 8,5 and lysosomal and nonlysosomal peptide hydrolase activity have been studied in brain and liver tissues of rats. L-arginine has been found to increase the peptide hydrolase activity in neutral and alkaline media in case of autolysis and proteolysis estimation according to the amino nitrogen increase. When the peptide hydrolase activity is estimated according to the increase of folin-positive components its decrease under the action of arginine in neutral and alkaline media has been revealed. Arginine doesn't change the lysosomal peptide hydrolase activity. In both tissues under the influence of arginine the nonlysosomal peptide hydrolase activity defined by amino nitrogen increases, estimated by the folin-positive components--decreases. Arginine shows the specific influence on the nonlysosomal peptide hydrolase activity. The L-arginine analogues (D-arginine, guanidine) and products of the arginase reaction (ornithine and urea) don't exert such an effect on the nonlysosomal proteolysis.