Modern medicine now encounters with problem of the absence of effective antibacterial drugs, which are able to render therapeutic effect on chronic form of infectious process. Thus, the actual objective is to develop essentially new generation of drugs, on the basis of which should lie identification of new bacterial targets playing key role in process of chronization of infection as well as selection of new physiologically active substances, which are able to render highly specific inhibitory effect on selected target. Solving of this objective is possible during realization of new approaches for search and design of new drugs and, first of all, during usage of bioinformatics methods, which enable to identify new biotargets, select most effective chemical compounds-inhibitors and optimize their pharmacological and pharmacokinetic properties.
View Article and Find Full Text PDFAcetates of 3beta-hydroxy-3'-methyl-1'(N)-acylandrost-5-eno[16,17-d]pyrazolines bearing monothiooxamide acyl groups were synthesized during the study of approaches to the synthesis of 3'-methylandrosteno[16,17-d]azoles, promising biologically active analogues of 20-keto pregnenanes, and their properties were investigated. The cyclization of delta16-20-thiooxamidohydrazones to the corresponding heterocycles was shown to proceed under rigorous conditions and to depend partially on the nature of the oxamide grouping.
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May 1985
Regularities of protease and alpha-amylase production by washed cells of Aspergillus oryzae 251-90 were being studied. The results obtained enabled us to assume a constitutive character of the both enzymes synthesis by the given producer. Sources of carbon, nitrogen and sulphur take part in regulation of the protease production, whereas in the case of the alpha-amylase synthesis only carbon sources that are important.
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May 1980
Commercial glucoamylase was immobilized on the polymer carrier produced by the binding of 4--8 mol.% 4,4'-diamine diphenyl oxide of the maleic anhydride copolymer with N-vinyl pyrrolidone. Two types of immobilized preparations were obtained: with covalent absorption and covalent attachment of the enzyme to the polymer.
View Article and Find Full Text PDFGrowth of the yeast-like fungus Endomycopsis fibuliger 55-13 during continous cultivation was studied. The microorganism produced amylolytic enzymes during flow cultivation. As a result of the three-stage cultivation the productivity increased two-fold and the time of cultivation decreased by 6 hrs as compared with periodic cultivation.
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September 1978
The effect of different sources of carbon and other components on the glucoamylase synthesis by Endomycopsis fibuligera 21 was investigated. It was demonstrated that the enzyme was actively synthesized after the complete utilization of the carbon sources and the synthesis was not related to the presence of specific substrates in the medium. It was shown that water immersed washed cells of the producer accumulated high glucoamylase activity.
View Article and Find Full Text PDFThe study of spontaneous variation of Act. werraensis not subjected to the treatment with mutagens and stabilizing selection revealed 6 variants within the homologous series of hereditary variation of apigmental actinomyces. The example of revealing the proactinomycete-like variants in Act.
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July 1977
The effect of temperature and different carbon sources on the growth of Bacillus species and the synthesis of alpha-amylase was studied. The temperature of 40 degrees proved to be optimal for those processes. Starch was found to be the best carbon source.
View Article and Find Full Text PDFAction of transglucosilase from Asp. batatae on different substrates is studied. The ratio of transglucosilase (upsilont) and hydrolase (upsilonh) activities on maltose under the action of transglucosilases from different origins is estimated.
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January 1976
The enzymic preparation isolated by ethanol precipitation from the aqueous extract of the surface culture of Aspergillus terricola was purified on biogel P-10, fractionated on SE-Sephadex. As a result, 10 fractions of acid proteinases that differed in pH optima and activity were obtained. After purification specific activity of some fractions per 1 mg protein increased 24-32-fold.
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