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The aim of this study was to determine trypsin-lake proteinase activity, chymotrypsin-like proteinase activity, trypsin, alpha 1-antitrypsin and alpha 2-macroglobulin levels in blood serum at the children with gastroenterological pathology. These parameters did not chang at the children with functional disorder of stomach and duodenum. The stable balance between proteinases and inhibitors was determined only at the duration of the disease not more 5 years. The absence of normal levels these enzymes after traditional treatment was explain the necessity to continue the therapy at home with control of enzymes' levels.

Protease activities in serum and urine of 116 children with glomerulonephritis and 16 healthy children were tested using chromogenic peptide substrates Z-Dala_Leu-Arg-pNA and Glp-Ala-ALa-Leu-pNa. We found the dependence between activity of serine proteinases and clinical, morphological forms of primary glomerulonephritis and hypertension.

The authors treated destructive forms of acute pancreatitis for the first time by means of specific plasma sorption of proteinases with the use of a proteinase plasma sorbent which is an acid-stable proteinase inhibitor immobilized on sepharose (ASI-Sepharose). Specific plasma sorption of proteinases on ASI-Sepharose was applied to the treatment of 29 patients with various forms of acute destructive pancreatitis. At the end of specific plasma sorption procedure the activity of blood plasma proteolytic enzymes in the patients reduced by 60-75%, which was attended by marked improvement of the condition in most cases; aggravation of the patients' condition was not encountered. The mortality in this group was 20.7% and was due to complications occurring during the development of the main disease. The mortality rate among patients treated by specific proteinase plasma sorption is much lower than that recorded in the USSR for destructive forms of acute pancreatitis which ranges from 30 to 75%.

Proteinase-inhibitor balance in human plasma before and after artificial blood circulation was examined. It was shown that trypsinlike and chemotrypsinlike proteinases activities after this procedure were 1.6 and 2.8 times higher and antitryptic activity 1.2 times lower than in the same patients before the procedure. The 40-50% decrease of proteinase activity in human plasma after artificial blood circulation was observed as a result of in vitro plasmasorption on immobilized human urinary trypsin inhibitor.

Data on biochemistry, physiological significance and clinical investigations of two main inhibitors of proteinases in human blood serum (alpha 1-antitrypsin and alpha 2-macroglobulin) are reviewed. Physico-chemical properties of the inhibitors, mechanisms of their interaction with proteinases and methods for determination are discussed. Modification of the specificity of some proteinases by alpha 2-macroglobulin, which probably plays a significant role in the regulation of enzymatic systems of proteolysis in blood, is considered. The use of the inhibitors of proteolysis for diagnostics of pathological processes is discussed. Data on the alpha 1-antitrypsin deficiency and its relation to the development of degenerative diseases in lungs are reviewed.

Role of granulocyte proteinases and their inhibitors, found in bronchial secretions, in pathogenesis of bronchopulmonary diseases is discussed. The acid-stable inhibitors, synthesized in bronchi, were responsible mainly for the antileukoproteinase effect in upper respiratory tract and bronchi. Influence of alpha 1-inhibitor of proteinases and other blood plasma labile inhibitors on destructive impairments in bronchopulmonary tissue is considered. Use of proteinase inhibitors as therapeutic drugs in bronchopulmonary pathologies is discussed.

Blood serum separation by the method of gel filtration on Sephadex G-200 with the subsequent immunochemical determination of the quantitative content of basic proteolysis inhibitors permitted isolating the alpha 2-macroglobulin fraction while alpha 1-antitrypsin and alpha 1-antichymotrypsin separation was a failure. The immunochemical analysis of the antienzymic activity of the isolated inhibitors showed that 32.3 +/- 3.5% of the introduced kallikrein, 18.7 +/- 0.6% of trypsin and 14.4 +/- 4.1% of chymotrypsin were bound in the zone of alpha 2-macroglobulin. The rest of antienzymic activity was localized in the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin. After a preliminary saturation of blood serum with trypsin in the amount equivalent to its antitryptic capacity (200 micrograms/ml) the ability of alpha 2-macroglobulin to bind kallikrein and chymotrypsin lowers considerably (by 69 and 72%, respectively). In the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin a decrease in the ability to bind kallikrein and chymotrypsin amounted to 44 and 12% respectively. Thus, alpha 2-macroglobulin being bound with trypsin looses considerably its ability to bind other enzymes.

The data obtained allow to consider urine acid-stable proteinase inhibitor (ASPI) activity as an early and informative index of renal parenchyma damage in patients with renal symptomatic arterial hypertensions without significant urine changes. Urine ASPI activities seems to be useful in differentiation of patients with chronic glomerulonephritis without significant urine changes and patients with hypertensions.

An effective method of plasma proteinases (trypsin, chymotrypsin. elastases) removal in dogs with acute pancreatitis has been suggested. The method is based on plasmasorption, using human urine acid-stable proteinase inhibitor immobilized on sepharose. The procedure of plasmasorption reduces proteinase levels in dogs with acute pancreatitis to 35-70%, with the animal life-span prolonged 8-fold.