[Effect of synthetic fragments of thymic peptide hormones on learning and memory processes]. / Vliianie sinteticheskikh fragmentov peptidnykh gormonov timusa na protessy obucheniia i pamiati.

Seven synthetic peptide fragments of thymic hormones were investigated using behavioral and electrophysiological methods. Splenopentin was shown to increase markedly learning capacities and memory. In contrast, alpha 1-thymosin fragment decreased them. Other peptides only slightly affected the capacities. Two active peptides seem to affect the level of activation of subcortical structures responsible for the excitation and inhibition.

[The role of ACTH(5-8) and beta-MSH(5-8) fragments in the organization of the self-stimulation reaction]. / Uchastie fragmentov ACTH(5-8) i beta-MSH(5-8) v organizatsii reaktsii samorazdrazheniia.

The experiments on rats have shown that intraperitoneal administration of ACTH5-8 fragments in a dose of 40 ng per kg altered considerably the character of self-stimulation reaction and the behaviour of rats. Searching activity and self-stimulation reaction were intensified, with the latter characterized by the onset of aversive components, that disappeared 24 hours later. Activation depended on the site of stimulation. Two phases of activity were noted (the first 0.5-1 h and the second 4.5-6 h after ACTH5-8 injection). beta-MSH5-8 fragment, when injected intraperitoneally in a dose of 20 ng per kg, had no effect on self-stimulation reaction and the behaviour of animals.

[Effect of beta-lipoprotein derivatives on the drinking and feeding behavior of rats]. / Vliianie riada proizvodnykh beta-lipotropina na pit'evoe i pishchevoe povedenie krys.

The effects of some previously unexplored beta-lipotropin derivatives (fragments of beta-MSH 4-7 and 5-8 corresponding to fragments of beta-lipotropin 40-43, 41-44; an enkephalin analog--an enkephalin-like tetrapeptide Tyr-D-Ala-Gly-Phen-NH2) on drinking and food behavior of rats were studied and compared. beta-MSH 5-8 was found to possess a remarkable dipsogenic action but to produce no effect on food intake in rats. At the same time a structurally related analog beta-MSH 4-7 and enkephalin-like tetrapeptide did not alter drinking behavior of animals, exerting, however, a substantial satiating action on hungry rats and initiating food behaviour in fed animals. The effects of the peptides on drinking and food behavior appeared long-term, persisting for 14-16 days and even up to 4-4.5 months upon administration of the enkephalin-like tetrapeptide. The data obtained suggest that the structural similarity of peptides does not always determine the common characteristics of their physiological effects which depend to a considerable degree on the initial food motivation.

[Identity of kininogenase and plasminogen activators in human granulocytes]. / K voprosu ob identichnosti kininogenazy i aktivatora plazminogena granulotsitov cheloveka.

It was shown that the plasminogen activator inhibitor, ZGlyGlyArgCH2Cl, inactivates the kininogenase and plasminogen activator activities in the whole human granulocyte lysate and human granulocyte proteinase fractions isolated by isoelectrofocusing from the granulocyte lysate (pH 3-10). The kinetics of irreversible inhibition of the ZGlyGlyArgpNA-amidase activity in granulocyte proteinase fractions (pI 10.75, 8.9 and 8.3) by ZGlyGlyArgCH2Cl was measured. These data confirm the earlier obtained results on the trypsin-like nature of the human granulocyte plasminogen activator and its identity to this cell kininogenase.

[Inhibition of human granulocyte elastase and kininogenase]. / Ingibirovanie élastazy i kininogenazy granulotsitov cheloveka.

Using an inhibitory analysis, the different enzymatic nature of kininogenase and elastase activities in serine proteinase fractions (pI 8.3-10.75) isolated from human granulocyte lysates by isoelectrofocusing was demonstrated. The thermo- and acid-stable serine proteinase inhibitor from rabbit serum was shown to completely inhibit the kininogenase activity in these fractions but to have no inhibiting action on the elastase activity. On the contrast, the specific granulocyte elastase inhibitor, N-3-carbomethoxypropanoyl-L-alanyl-L-alanyl-L-prolyl-L-valyl-chloromethylketone , inhibits granulocyte elastase and does not inhibit the kininogenase activity in lysate fractions. The efficiency of granulocyte elastase inhibition by this chloromethylketone is evaluated by the kinetic parameters k3, Ki. The values of k3/Ki for granulocyte elastase forms with pI of 10.75, 8.9 and 8.0 are 1430, 670 and 360 M-1 S-1, respectively and show effective inhibition of the three forms by this inhibitor. Based on the different degree of inhibition of the three elastase forms by chloromethylketone inhibitor the existence of the family of elastaselike enzymes in human granulocytes is postulated.

[Identity of human granulocyte kininogenase and plasminogen activator]. / Ob identichnosti kininogenazy granulotsitov cheloveka s aktivatorom plazminogena.

Preparative isoelectrofocusing used for fractionating the whole human granulocyte lysate serine proteinases revealed multiple forms of elastase, cathepsin G, kininogenase, human granulocytes plasminogen activator (pI 6.2-10.75). Kinetic characteristics of their substrate specificity were also obtained. It is shown that serine kininogenase of human granulocytes is not identical with elastase as it had been supposed before, it is of trypsin-like nature and is identical with plasminogen activator of these cells. The results obtained reveal new aspects in comprehension of the role of the granulocyte plasminogen activator in development of the inflammatory reaction. It is found that acid-stable proteinase inhibitors formed from blood plasma inter-alpha-inhibitor of trypsin, have an inhibitory effect on the granulocyte plasminogen activator, that supports an assumption on the anti-inflammatory function of these inhibitors.

[Preparation of subtilisin BPN' and dextran conjugates]. / Poluchenie konbiugatov subtilizina VPN' s dekstranami.

The conditions for subtilishine BPN' binding with bromocyanogen activated dextranes have been selected. The dependence of the enzyme activity and stability from pH and temperature levels has been studied. The stability of a modified enzyme during storage in solution is increased as compared with that of the native enzyme due to a decrease in the autolysis rate. On the basis of diffusion coefficients and sedimentation constants of conjugates, absolute values of their molecular weights have been computed.