SOME ASPECTS OF A SPECIFIC AND HIGH-SENSITIVE DETEC- TIONS OF CHYMASE ACTIVITY IN THE ASSESSMENT OF PHARMA-COTHERAPY EFFICIENTLY
The optimal conditions for highly sensitive determination of chymase activity in biological fluids using an effective competitive inhibitor of proteinases were selectedand analysis of research capabilities of its activity in humans and some animals were held. It is shown that the use for the proteolytic reactions of complex of horseradish peroxidase with a fragment of angiotensin II 5-8 and of angiotensin II 4-8 at the its immobilization in a concentration of 30 µg/ml, and early inhibition of trypsin-like enzymes by the action of soybean trypsin inhibitor at a concentration of 0.01 µg/ml for 5 minutes allows specific determination of chymase activity in biological fluids of humans and animals.Investigation of chymase activity in human serum revealed its level (1,073+0,294) E x 10-3. In the non-nuclear fractions of tissues of old rats it level was naturally much smaller and had a tissue-specific character. The manifestation of tissue specificity and less chymase activities in tissue samples as compared with rats found in hamsters. It is shown that the determination of chymase activity may be useful in the study of age-specific features of its involvement in the pathogenesis of diseases of the internal organs. The diverse character of the possible changes of chymase activity in the pathology is causes the necessitates of informed destination and control of the use of drugs.Many side effects of known pharmaceuticals is encourages scientists to search for new safe and effective means of control of angiotensin II in the organism. The use of this method of determining the activity of chymase to evaluate the effectiveness of new drugs, particularly for the treatment of hypertension, will contribute to the prevention of harm to the target organs.