[Prognostic power of various models in determination of level of coronary risk in patients with non ST-elevation acute coronary syndrome].

The GRACE prognostic scale appeared ineffective for prognostication of deaths and sum of deaths and myocardial infarctions (MI) during hospitalization and demonstrated moderate level of prognostic value during 6 months of observation. TIMI model gave similar result relative to prediction of death/MI/refractory ischemia during 14 days and 12 months of observation. PURSUIT risk model showed very good level of prognostic significance during 30 days and 12 months of observation. Comparison of GRACE and PURSUIT models relative to all cause death and composite of death and MI showed that PURSUITd scale had better accuracy of predictions.

[Modification of the ortho-route in Pseudomonas putida strain 87: purification and properties of dienlactone hydrolase]. / Modifitsirovannyi orto-put' u shtamma Pseudomonas putida 87: ochistka i svoistva dienlakton gidrolazy.

Dienelactone hydrolase (DLH) was purified to electrophoretic homogeneity from the biomass of the Pseudomonas putida strain 87 grown on 3-chlorobenzoate. The specific activity of the purified enzyme is 50.5 U./mg of protein. The enzyme is a monomer with a molecular mass of 22 kDa, has a pH optimum at 7.6 and is active within a broad temperature range (20-45 degrees C). The enzyme activity is inhibited by pCMB (which requires up to two equivalents of the reagent) but not by EDTA. The Vmax values of DLH for trans-dienelactone and 2-chlorodienelactone are practically identical (247.9 and 247 u./mg, respectively) and exceeded two fold that for cis-dienelactone. However, the Km for 2-chlorodienelactone is two times as high as that for trans-dienelactone (6.9 and 14.2 microM, respectively). A comparison of physico-chemical and kinetic properties of P. putida 87 DLH with those of the enzymes responsible for the decomposition of chlorinated and fluorinated compounds revealed that the enzyme can be assigned to the third group, i.e., the DLH-modified ortho-cleavage path way characteristic of gram-negative bacteria.

[Purification and properties of pyrocatechase II from Pseudomonas putida strain 87]. / Ochistka i svoistva pirokatekhazy II iz shtamma Pseudomonas putida 87.

Induction of modified ortho-pathway enzymes (catechol 1.2-dioxygenase II, muconate cycloisomerase II, dienelactone hydrolase, and maleylacetate reductase) was found in Pseudomonas putida 87, when 3-chlorobenzoic acid was used as a sole carbon and energy source. Catechol 1.2-dioxygenase II, the key chlorocatechol cleaving enzyme, was purified and characterized. The enzyme molecular mass as determined by gel filtration was 65,000 Da; the minimum molecular mass upon SDS electrophoresis was 33,000 Da. The pH and temperature optima for the enzyme were 7.2-7.8 and 35 degrees C, respectively. The highest stability of catechol 1.2-dioxygenase II upon storage was observed in 50 mM Tris-HCl buffer pH 7.8 at 4 degrees C. The relative values of Vmax for catechol 1.2-dioxygenase II with 3-chloro-, 4-chloro-, and 3.5-dichlorocatechols were 28%, 50%, and 41% of those for catechol. The enzyme affinity for chlorocatechols was 3-9 times higher than for methylcatechols and 10-20 times higher than for unsubstituted catechol.

[Peripheral metabolism of Pseudomonal putida transconjugants degrading chloro- and methylaromatic compounds]. / Periferiinyi metabolizm transkon''iugantov Pseudomonas putida, razlagaiushchikh khlor- i metilaromaticheskie soedineniia.

Peripheral metabolism was studied in the Pseudomonas putida 37cc transconjugant. In the strain grown on benzoate, pyrocatechase (PC) I with a low activity to chlorocatechols was induced, whereas PCII actively decomposing chlorocatechols was induced during its growth on 3-chlorobenzoic acid. The P. putida 37cc transconjugant grown on alpha-methylstyrene (MS) exerted the activity of both metapyrocatechase (MPC) and PC, whereas in the parent strain P. putida R-1 only MPC was involved in the degradation of alpha-MS. The substrate specificity of the enzymes involved in the ring cleavage by P. putida 37cc was compared to show that, apparently, MPC of the transconjugant was similar to this enzyme in the strain R-1 while PC decomposing chlorocatechols was similar to PC of the P. putida 87 donor. The regulation of the enzymes mediating the ring cleavage was studied in the parent strains and transconjugants.

[Role of additional substrates in DDT degradation by cultures of Pseudomonas aeruginosa]. / Izuchenie roli dopolnitel'nykh substratov pri degradatsii DDT kul'turoi Pseudomonas aeruginosa.

The activity of enzymes was compared during Pseudomonas aeruginosa 640x growth on compounds activating DDT to a different degree and on acetate which did not stimulate this process. The activity of dehydrogenases generating reduced cofactors necessary for DDT dechlorination was found to be much higher on effective additional substrates than on compounds which either had no effect on DDT degradation or stimulated this process only slightly. The activity of enzymes generating the reduced cofactors was shown to correlate with the extent of DDT degradation by this culture.

[Central metabolic characteristics of a Pseudomonas aeruginosa culture degrading DDT]. / Osobennosti tsentral'nogo metabolizma kul'tury Pseudomonas aeruginosa, degradiruiushchei DDT.

The object of this work was to investigate the operation of enzymes of the citric acid cycle, the glyoxylate pathway, the glucose metabolism as well as of pyruvate and phosphoenolpyruvate carboxylases in Pseudomonas aeruginosa 640x capable of complete degradation of DDT under the conditions of cometabolism. The activity of isocitrate and glucose-6-phosphate dehydrogenases producing reduced NADP, which is required for reductive dechlorination of DDT, appears to be high. Pyruvate carboxylase and phosphoenolpyruvate carboxylase (EC 4.1.1.31.) function simultaneously in the culture. Differences in the pathways of anaplerotic carbon dioxide fixation were found in P. aeruginosa 640x and the collection strain of P. aeruginosa PAO incapable of DDT degradation.