[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.

Thermodynamic approach to the selection of polyuronide sequestrants for preventive and medicinal nutrition.

An approach to the analysis of isotherms of cooperative binding is developed that allows to calculate approximately affinity profiles, i.e. dependencies of binding constants on binding densities.

Conformational stability of bovine holo and apo adrenodoxin--a scanning calorimetric study.

Holo and apo adrenodoxin were studied by differential scanning calorimetry, absorption spectroscopy, limited proteolysis, and size-exclusion chromatography. To determine the conformational stability of adrenodoxin, a method was found that prevents the irreversible destruction of the iron-sulfur center. The approach makes use of a buffer solution that contains sodium sulfide and mercaptoethanol.

2-Methyl-L-tryptophan is a substrate of tryptophanase.

Tryptophanase was generally considered to be inactive towards tryptophan derivatives substituted at 2-position of the indole ring. We have shown that cells containing tryptophanase catalyze the formation of 2-methyl-L-tryptophan from 2-methylindole and L-serine, and from 2-methylindole, pyruvate and ammonium ion. The kinetics of pyruvate formation from 2-methyl-L-tryptophan and its alpha-deuterated analogue catalyzed by homogeneous tryptophanase were examined.

Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.

In water-methanol and water-dimethylformamide (DMF) (1:1 v/v) solutions tryptophanase from E.coli retains its abilities to form a quinonoid complex with quasisubstrates and to catalyze the decomposition of S-o-nitrophenyl-L-cysteine (SOPC). Both the KM and Vmax values decrease in water-organic media.

Chitinolytic digestibility of cross-linked chitosan gels by an enzyme complex from Streptomyces kurssanovii.

The action of a microbial chitinolytic enzyme complex from Streptomyces kurssanovii on chitosan gels with various degrees of cross-linking and on the O-derivatives of the gels was examined. The rate of digestion of the gels was shown to depend on the degree of cross-linking as well as on the size of the O-substituent, decreasing greatly with a rise in substitution.