RESUMEN
As a result of research it is proved, that the most significant factors of competitiveness are quality of rendered medical services. All can be estimated the necessary parties of quality on the basis of medical standards. The technique of an estimation of quality of out-patient medical aid consists in comparison of the standard of groups of parameters of quality (diagnostics, treatment, results), considering their factors of weightiness) with real data of concrete patients.
Asunto(s)
Atención a la Salud , Competencia Económica , Hospitales Militares , Medicina Militar , Garantía de la Calidad de Atención de Salud , Atención a la Salud/economía , Atención a la Salud/métodos , Atención a la Salud/normas , Hospitales Militares/economía , Hospitales Militares/organización & administración , Hospitales Militares/normas , Medicina Militar/economía , Medicina Militar/organización & administración , Medicina Militar/normas , Federación de RusiaRESUMEN
Restriction map of Escherichia coli chromosome fragment (7.4 MD) carrying proAB genes was constructed. Localization of proA and proB genes on the cloned chromosome fragment was determined by complementation test and the measuring of glutamylkinase activity (proB gene product). ProA and proB genes were cloned separately on multicopy plasmids of alternative orientation and their expression being, probably, under the control of their own regulatory regions, studied.
Asunto(s)
Clonación Molecular , Escherichia coli/genética , Genes Bacterianos , Prolina/biosíntesis , Enzimas de Restricción del ADN , Escherichia coli/metabolismo , Plásmidos , Prolina/genéticaRESUMEN
ArgA and argECBH genes of Escherichia coli K-12 were cloned on the pBR322 vector. Restriction maps of the recombinant plasmids were constructed. Deletion mutants of these recombinant plasmids, retaining the functional argA and argE genes, were obtained using different restriction enzymes. All of the recombinant derivatives have the replication properties of the pBR322 vector.
Asunto(s)
Arginina/biosíntesis , Escherichia coli/genética , Genes Bacterianos , Plásmidos , Recombinación Genética , Mapeo Cromosómico , Enzimas de Restricción del ADN , Escherichia coli/metabolismoRESUMEN
A comparative study of the inhibitory effect of clorgyline and deprenyl on serotonin, beta-phenylethylamine and tyramine deamination by intact mitochondria as well as by solubilized with methylethylketone and partially purified monoamine oxidase (MAO) from rat liver was carried out. The effect of 4-ethylpyridine on this process was investigated. After solubilization of MAO by methylethylketone 7% of mitochondrial activity passes into solution and the rate of deamination of serotonin, tyramine and beta-phenylethylamine by soluble MAO preparation is selectively decreased. The corresponding residual activities are equal to 29, 63, 86 and 92%. The inhibitory effect of clorgyline on serotonin deamination by soluble MAO preparations is considerably lower than that by mitochondrial suspensions at the concentrations of the inhibitor from 1 x 10(-4) to 1 x 10(-7) M, while the inhibitory action of clorgyline on tyramine deamination after MAO solubilization by methylethylketone is increased at 10(-4) and 10(-5) M, but decreased insignificantly at 10(-6) and 10(-7) M. When solubilized MAO preparations are used, 4-ethylpyridine introduced into the sample before or after preincubation of the enzyme with clorgyline (30 min, 23 degrees) eliminates the inhibitory action of the latter on serotonin and tyramine deamination, thus suggesting the reversibility of the inhibitory effect of clorgyline. In similar experiments with mitochondrial suspensions the inhibition by clorgyline of deamination of these amines is irreversible. Similar experiments on mitochondrial suspensions showed that clorgyline irreversibly inhibits the deamination of these amines. The rate of inhibition by deprenyl of beta-phenylethylamine oxidation due to MAO solubilization by methylethylketone is not changed. 4-Ethylpyridine added to the samples before or after preincubation of deprenyl with the enzyme (30 min, 23 degrees) abolishes the inhibiting effect of the former both in soluble MOA and in mitochondrial suspensions. This suggests that under the given experimental conditions the inhibiting effect of deprenyl is reversible. Possible nature of MAO forms A and B is discussed.