[Conditions for cultivation of the fungus Penicillium melinii UzLM-4 and its biosynthesis of lipases]. / Usloviia kul'tivirovaniia i biosintez lipaz gribom Penicillium melinii UzLM-4.

Cultivation of the fungus Penicillium melinii UzLM-4 on a Raistrick's medium of our own modification made it possible to increase the biosynthesis of lipases three to four times. The following conditions ensured a high rate of synthesis of the extracellular lipase: age of the inoculum, 15 days; concentration of the inoculum, 15 x 10(6) conidia per 100 ml medium; initial pH of the nutrient medium, 8.0; and cultivation in a shaker at 150 rpm (25 degrees C).

[Change in phospholipid composition of synovial fluid in children with various types of arthritis]. / Izmenenie fosfolipidnogo sostava sinovial'noi zhidkosti u detei s razlichnymi artritami.

Phospholipid composition of synovial fluid was studied in patients with reactive, rheumatoid and juvenile chronic forms of arthritis as compared with that of normal synovial fluid. The most pronounced alterations of the synovial fluid phospholipid composition (additional phospholipid fractions, increase in content of lyso-derivatives) were found in the patients with rheumatoid and juvenile chronic arthritis, which appear to occur due to activation of endogenous phospholipases A2, C and lysophospholipase A1.

[Various lipases for producing products enriched with polyenic acids in fish fat hydrolysis]. / Issledovanie razlichnykh lipaz dlia polucheniia produktov, obogashchennykh polienovymi kislotami pri gidrolize rybikh zhirov.

The enzymic hydrolysis of fish with lipases from various sources was studied. The lipase from the fungus Rhizopus microsporus preferentially removes saturated fatty acids, while lipase from the pyloric caeca of salmon unsaturated fatty acids upon hydrolysis of fish fats. The enzymes can be used to obtain fatty products enriched with eicosanopentaenoic acid, mono- and diacylglycerols by enzymic hydrolysis of the ivasi fat.

[Purification and properties of lysophospholipase from the venom of the giant hornet Vespa orientalis]. / Ochistka i svoistva lizofosfolipazy iz aida bol'shogo shershnia Vespa orientalis.

Using biospecific chromatography on polylysocephamide, a toxic phospholipase possessing a presynaptic effect on neuromuscular preparations was isolated from the venom of the giant hornet Vespa orientalis. The enzyme was shown to possess a high hydrolytic activity towards 1-acyllysophosphatidylcholine within a narrow pH range (pH optimum 7.5). The enzyme activity was suppressed by detergents of various chemical composition. Lysophospholipase caused an intensive hemolysis of washed human erythrocytes. The catalytic and hemolytic functions of the enzyme were sensitive to metal ions, however, in a different degree. Ca2+ and Mn2+ activated, while Cu2+ and Zn2+ inhibited the enzyme. Mg2+ and Sr2+ had no effect on the enzyme activity.

[Biospecific adsorption chromatography of phospholipase A2 from different sources]. / Biospetsificheskaia adsorbtsionnaia khromatografiia fosfolipazy A2 iz razlichnykh istochnikov.

Methods of biospecific adsorption chromatography of phospholipase A2 obtained from porcine pancreas and Naja naja oxiana, Vipera ursini renardi, Vespa orientalis venoms were developed. Granulated polyamide with covalently linked phosphatidylethanolamine were used as an affinity adsorbent. Chemical inertness of linked phosphatidylethanolamine to the hydrolytic action of phospholipase A2 and its high affinity for biospecific complexes are shown. Forms of phospholipase A2 different in their affinity for an immobilized substrate was isolated by biospecific adsorption chromatography. The role of hydrophobic and electrostatic interactions in formation of enzyme-ligand complexes was studied.

[Properties of phospholipase A2 from the venom of the large hornet Vespa orientalis]. / Svoistva fosfolipazy A2 iz iada bol'shogo shershnia Vespa orientalis.

Some properties (catalytic and hemolytic activity, pH and temperature optima, stability, substrate specificity, effects of detergents and metal ions, N-terminal sequence, chemical modification of histidine in the enzyme active center, etc.) of phospholipase A2 from hornet (Vespa orientalis) venom were studied. It was shown that phospholipase A2 from hornet venom differs essentially from other enzymes of this species in terms of stability, catalytic properties and structural features. The active center of the enzyme contains an essential histidine residue, similar to other phospholipases A2 from various sources. Unlike other known forms of phospholipase A2, the enzyme under study exerts a pronounced hemolytic action. The hemolysis is inhibited by Ca2+ at concentrations capable of inducing the activation of the hydrolytic activity of the enzyme.