Inhibition of Proteolysis in Plant and Animal Tissues
Agrobiodiversity for Improving Nutrition, Health and Life Quality
Download Full-Text PDF


proteolysis; antiproteolysis; amidase reaction; docking; Phaseolus vulgaris; Lymnaea stagnalis; Planorbarius corneus

How to Cite

Chirkin, A., & Dolmatova, V. (2017). Inhibition of Proteolysis in Plant and Animal Tissues. Agrobiodiversity for Improving Nutrition, Health and Life Quality, (1). Retrieved from


The aim of the study was a comparative analysis of the alpha-1-antitrypsin and the alpha-2-macroglobulin content in 6-day seedlings Phaseolus vulgaris L. and hepatopancreas Lymnaea stagnalis L and Planorbarius corneus L. Quantification of proteinase inhibitors (α1-antiprotease inhibitor and α2-macroglobulin) was performed according to a method based on BAPNA-amidase reaction at pH values of incubation media of 3.0; 3.8; 6.1; 7.2; 8.0 and 9.0. It has been found that Phaseolus vulgaris cotyledons contain more alpha- 1-antiprotease inhibitors that work in acidic, neutral and alkaline media compared to similar inhibitors of molluscs hepatopancreas. At pH 3.8, the content of alpha-2-macroglobulin in the cotyledons of Phaseolus vulgaris is 8 times higher than the levels of this inhibitor in the hepatopancreas of molluscs. The sites of ethionine binding with human trypsin and pulmonary freshwater molluscs are located in close loci at the C-ends of the enzyme molecules, which allows to consider these animals as potential model organisms for biopharmaceutical studies of the proteolysis-antiprotеolysis system.

Download Full-Text PDF


Download data is not yet available.