Immunochemical analysis in combination with gel filtration and isoelectric focusing made it possible to state that in blood serum of healthy people 81.3 +/- 0.5% of administered trypsin is bound with alpha 1-antitrypsin and 18.7 +/- 0.6%--with alpha 2-macroglobulin. The latter is functionally heterogeneous, only 40% of it is bound with trypsin and in the formed complex the antigenic properties of trypsin and alpha 2-macroglobulin are lost. A great number of blood serum alpha 1-antitrypsin cannot fix trypsin. The content of such alpha 1-antitrypsin rises sharply with pathology available. In the immunochemical estimation of the organism inhibitory potential relative to proteolytic enzymes not only the amount of the inhibitor but also its functional activity should be taken into account. The data of immunochemical research of the blood serum isoelectrophoregrams show that the most considerable changes under conditions of pathology occur in alpha 2-macroglobulin.

Humans↗

PubMedDate not supplied

[Proteolytic enzyme inhibitor and the kinin system in thyrotoxicosis].

Free bradykinin, kininogen, kininase, protease inhibitors of alpha 1-antitrypsin, alpha 1-antichymotrypsin, alpha 2-macroglobulin, and antitryptic volume of the blood serum were examined in 25 patients suffering from goiter with thyrotoxicosis symptoms. Activation of the kinin system and reduction in the antitryptic volume were revealed before the operation. The level of the rest inhibitors was elevated. After operative intervention these changes became more expressed. alpha 2-Macroglobulin content increased. By the moment of discharge the above parameters tended to normalization. The content of the majority of inhibitors, however, did not reach normal. This should be taken into consideration during rehabilitation of patients with thyrotoxicosis.

Adult↗

PubMedDate not supplied

[Effect of proteolysis enzymes and their inhibitors on oxygen uptake by rat brain tissue and its antitryptic activity].

Trypsin in a dose of 3 microgram increases the intensity of oxygen uptake and antitryptic capacity of the brain tissue in animals under study. These indices decrease considerably under the effect of trypsin in a dose of 6-12 microgram. Kallikrein in the same doses has a unidirected stimulating effect. The antitryptic serum and ingitryl block the biological effect of trypsin and similarly to the rabbit normal and antikallikreinic serum stimulate the oxygen uptake.

Animals↗

PubMedDate not supplied

[Effect of proteolysis inhibitors on serum proteinase activity and its antitryptic activity in postischemic toxemia].

Parenteral administration to animals of the antikallikrein serum containing 200gamma/ml of antibodies to the pancreatic kallikrein (10 ml/kg), ingitryl (1.5 Un/kg) and of tracilol (10 000 Un/kg) exerts in post-ischemic toxemia an inhibiting effect on the protamine-splitting blood serum activity and does not affect the benzoylarginine-paranitroanilide rate of splitting. Changes of the blood serum ability to bind trypsin and manifestation of the protamine-splitting activity during the first 9 hours of observation are of an undulating nature and the changes of these characteristics are reciprocal.

Animals↗

PubMedDate not supplied

[Immunochemical assessment of the antigenic relationship between the pancreatic kallikrein of rodents and carnivores].

Using quantitative and qualitative immunochemical methods, in combination with isoelectrical focusing, it was shown that antibodies to commercial kallikrein are involved into precipitation reaction with kallikrein in extracts from the pancreas of dogs, cats, guinea pigs, rats and mice. Complexes antigen--antibody exhibit similar physico-chemical properties; during isoelectric focusing, they are found in the same pH range as the immunoactive portion of commercial kallikrein. These data indicate antigenic similarity of pancreatic kallikrein in different mammalian species.

Animals↗