[The use of polyelectrolytes for isolation of trypsin inhibitor from industrial waste of fractionation of alfalfa leaf proteins].

Arypsin inhibitor was concentrated from the albumin fraction of alfalfa leaf juice as insoluble complex precipitate with pectin, carboxymethylcellulose sodium salt, and dextran sulfate. The concentration degree varied from 40 to 100, and the yield of the inhibitor was 45-50%. The homogeneous inhibitor was further isolated from solution of the precipitate by affinity chromatography on Trypsin-Sepharose. The final product had a molecular weight of 6.9 kDa, high inhibitory activity (16.6 U per mg protein) and relatively high (about 30%) content of the alpha-helical form.