[Experimental morphological study of the therapeutic effect of shark cartilage preparation in a model of infective allergic arthritis].

The therapeutic effect of a Polar shark cartilage preparation which is an enzymatic hydrolysate was studied in a rabbit model of infective allergic pseudotuberculous arthritis. Characterization of the chemical composition of the preparation designed by an original method is presented. Improvement of the general state of the affected joints and development of tissue immunomorphological responses were shown.

[Activity of proteolytic and nucleolytic enzymes from the gonades of hydrobionts]. / Aktivnost' proteoliticheskikh i nukleoliticheskikh fermentov v gonadakh gidrobiontov.

The activity of nucleolytic and proteolytic enzymes in milt of nine kinds of fishes belonging to various families and of three kinds invertebrates is determined. There is carried out electrophoreses division of preparations DNA, received from milts by various methods; there are determined structure and molecular weights of oligonucleotides. The influence of activity tissue enzymes on a destruction degree of DNA is established at addition enzymes of exogenic origin.

[Effect of endogenous enzymes on composition of oligonucleotides isolated from gonads of hydrobionts]. / Vliianie éndogennykh fermentov na sostav ologonucleotidov pri ikh vydelenii iz gonad gidrobiontov.

Preparations of low-molecular-weight DNA were obtained from gonads of various hydrobiont species by alcohol precipitation technique. An enzymatic hydrolysis-based method for producing soluble low-molecular-weight DNA was developed. All the nucleic acid components of the preparations obtained were separated by electrophoresis, and their molecular weights were determined. It was demonstrated that high activities of endogenous enzymes (nucleases and proteases) in milts of hydrobionts correlated with the degree of hydrolysis of their nucleic acids.

[Inhibitory effect of antimicrobial preparation from lipids of marine fishes on tissue and microbial enzymes]. / Ingibitornoe deistvie antimikrobnogo preparata iz lipidov morskikh ryb na tkanevye i mikrobnye fermenty.

We obtained a new food preservative from marine fish lipids possessing pronounced activity in relation to bacteria and microscopic fungi. The effects of this preparation on enzymes of microorganisms and muscle tissue of marine hydrobionts were studied. In vitro the preparation irreversibly inhibited acid and alkaline proteases and proteolytic and lipolytic enzymes of microorganisms and reduced enzyme activity in fish muscle tissue. The inhibitory effect of this preparation on enzymes contributes to stabilization of hydrolytic processes in meat of hydrobionts and suppresses microorganism growth in storage.

[Antiprotease and immunostimulating effect of peptide components isolated from cuticle of the chicken stomach]. / Antiproteaznoe i immunostimuliruiushchee deistvie peptidnykh komponentov, vydelennykh iz kutikuly kurinogo zheludka.

Peptides with molecular weights of 0.8 to 16 kDa were isolated from the keratinous envelope of chicken muscular stomach cuticle. The peptide preparation had a immunostimulating activity whose qualitative and quantitative traits made it comparable with the activity of known drugs of similar composition. In addition, the peptide preparation reversibly inactivated trypsin and activated chymotrypsin. A low-molecular-weight protein (14.1 kDa) was isolated from the peptide preparation by affinity chromatography on trypsin-Sepharose 4B. This protein was found to be a reversible noncompetitive inhibitor of trypsin.

[Enzymatic methods of preparation of protein hydrolysates by using proteolytic preparations of varying specificity]. / Fermentativnye sposoby prigotovleniia belkovykh gidrolizatov s ispol'zovaniem proteoliticheskikh preparatov razlichnoi spetsifichnosti.

The optimal conditions of enzymatic hydrolysis of proteins different composition and structure (protamin, casein, haemoglobin, fibrin, collagen) were established by using proteolytic enzymatic preparations with different specificity (pancreatin, pilrin, hepatopancreatin). The degree of hydrolysis, molecular and amino acid compositions of proteins were determined.

[Preparation and properties of trypsin from the pyloric caeca of Pacific Ocean salmon]. / Poluchenie i svoistva tripsina iz pilorichekikh pridatkov tikhookeanskikh lososei.

Trypsin from pyloric caeca of Pacific salmon was purified by affinity chromatography of the water extract on hexamethylenediamine-glycidylmethacrylate-cellulose. A protein band with a molecular weight of 22.5 kDa was found on SDS-electrophoresis in PAG. The protein band was homogeneous according to isoelectrofocusing in PAG (pI 4.0). The amino acid composition of the enzyme is typical of trypsin anionic forms; the major difference from the cationic forms is the lower content of lysine. The differences in properties caused by change of the enzyme molecule charge are similar to those observed in cationic trypsin when the lysine epsilon-amino groups of the latter are modified (change of pI, shift of the pH-optimum towards basic values, increase of stability to autolysis). Some natural trypsin inhibitors of the different origin suppressed the enzyme activity of trypsin from Pacific salmon in typical stoichiometric ratios. An unusual interaction of the enzyme with the specific inhibitor N-L-tosyl-L-lysine chloromethyl ketone was observed.

[Trypsin-, chymotrypsin-like proteinases in fishes]. / Tripsin-, khimotripsinpodobnye proteinazy ryb.

Recent data on the nature of trypsin-, chymotrypsin-like proteinases of fish are generalized. Localization and secretion of these enzymes in pyloric appendages of fish are considered in detail. Trypsin and chymotrypsin are in the state of proenzymes and transform into the active form by means of their own proteolytic factors. It is observed that the classical methods for isolation of individual chymotrypsin and trypsin cannot be used in the case of fish, since the fish enzymes are stable in the neutral and low-alkaline media and unstable in the acid medium. This is, first of all, accounted for by differences in the physicochemical characteristics of the test enzymes. New data on the biospecific chromatography of serine proteinases of lower invertebrates are presented. Biospecific sorbents used for isolating enzymes from mammals are not always convenient for purification of fish serine proteinases. This evidences for considerable differences in their active sites and, probably, in their binding sites, whose nature is responsible for the specificity and is important for the selective chromatography of enzymes.