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[Study of 14 denitrifying soil bacteria of the "pseudomonas stutzeri" group isolated by enrichment culture in the presence of nitrous oxide (author's transl)].

The strains were isolated from soil by enrichment in a liquid minimal medium containing ethanol, acetate, succinate, L-malate or tartrate, under an N2O atmosphere at 32 degrees C. All fourteen strains can use the following 25 sources of carbon and energy under aerobic conditions: glycerate, ethanol, propanol, acetate, butyrate, malonate, succinate, glutarate, sebacate, glycollate, L-lactate, D-lactate, L-malate, DL-3-hydroxybutyrate, pyruvate, fumarate, itaconate, mesaconate, crotonate, L-alpha-alanine, D-alpha-alanine, L-leucine, asparagine, L-tyrosine, and L-proline. They hydrolyze Tween 80 but not gelatin. Nitrate is used as nitrogen source. Nitrate reductase A and respiratory nitrite reductase are present. Four of the strains are clearly and easily distinguishable from the others on the basis of six characters: special morphology of colonies; in ability to use isovalerate and DL-valine, inability to use glucose, absence of exocellular amylase, and high level of metapyrocatechase. Their G + C content is 66-67%. One of the strains is distinct from the others by the yellow pigmentation of its colonies, its ability to use D-glucuronate, trehalose, D-sorbitol and citraconate, ability to grow at 4 degrees but not at 40 degrees, and a lower G + C content: 63%. One strain accumulates poly-beta-hydroxybutyrate. This work confirms the well-known, wide variability of the bacteria belonging to the P. stutzeri group. Denitrification by two of the strains was quantitatively studied using cell suspensions. Cells from NO-3-containing anaerobic cultures reduce NO-3, NO-2 and NO to N2O and N2; they reduce slowly N2O to N2. Cells grown in anaerobic cultures under N2O also reduce NO-3, NO-2 and NO to N2O and N2 but they reduce N2O rapidly to N2.

Culture Media↗

[Dependence of ammonia nitrogen utilization in rabbits on concentration of carbonic acid in tissues].

Under conditions of an increase in the carbonic acid concentration in blood of rabbits (experimental group) utilization of ammonia nitrogen administered to the organism intensifies and simultaneously the level of keto-acids in blood as well as of free amino acids and urea in the liver tissue increases. In these animals as compared to the control ones the content of glutamine in blood and in the liver tissue decreases; the level of alpha-glutarate and glutamate in the liver tissue increases and that of pyruvate lowers. An increase is also observed in reducing power of the liver and kidney cell cytoplasm.

Amino Acids↗

[Formation of hemichrome during reaction of hemoglobin with polar phosphatidylcholine derivatives].

Polar phosphatidylcholine derivatives [1-acyl-2-lyso-sn-glycero-3-phosphocholine, 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor), 1-acyl-2-glutaryl-sn-glycero-3-phosphocholine, and 1-acyl-2-azelaoyl-sn-glycero-3-phosphocholine], which are formed in biological structures by enzymatic and free-radical reactions, were studied as effectors of the conversion of methemoglobin and oxyhemoglobin into an oxidized low-spin form referred to as hemichrome. It is shown that all these phosphatidylcholine derivatives act as effectors in the course of the transition of met- and oxyhemoglobin to hemichrome. Among the compounds studied, phosphatidylcholine derivatives containing glutaric and azelaic acids residues have the greatest effect on the rate of hemichrome formation.

Hemeproteins↗

Newborn screening for inborn errors of metabolism: a systematic review.

OBJECTIVES. To establish a database of literature and other evidence on neonatal screening programmes and technologies for inborn errors of metabolism. To undertake a systematic review of the data as a basis for evaluation of newborn screening for inborn errors of metabolism. To prepare an objective summary of the evidence on the appropriateness and need for various existing and possible neonatal screening programmes for inborn errors of metabolism in relation to the natural history of these diseases. To identify gaps in existing knowledge and make recommendations for required primary research. To make recommendations for the future development and organisation of neonatal screening for inborn errors of metabolism in the UK. HOW THE RESEARCH WAS CONDUCTED. There were three parts to the research. A systematic review of the literature on inborn errors of metabolism, neonatal screening programmes, new technologies for screening and economic factors. Inclusion and exclusion criteria were applied, and a working database of relevant papers was established. All selected papers were read by two or three experts and were critically appraised using a standard format. Seven criteria for a screening programme, based on the principles formulated by Wilson and Jungner (WHO, 1968), were used to summarise the evidence. These were as follows. Clinically and biochemically well-defined disorder. Known incidence in populations relevant to the UK. Disorder associated with significant morbidity or mortality. Effective treatment available. Period before onset during which intervention improves outcome. Ethical, safe, simple and robust screening test. Cost-effectiveness of screening. A questionnaire which was sent to all newborn screening laboratories in the UK. Site visits to assess new methodologies for newborn screening. The classical definition of an inborn error of metabolism was used (i.e., a monogenic disease resulting in deficient activity in a single enzyme in a pathway of intermediary metabolism). RESEARCH FINDINGS. INBORN ERRORS OF METABOLISM. Phenylketonuria (PKU) (incidence 1:12,000) fulfilled all the screening criteria and could be used as the 'gold standard' against which to review other disorders despite significant variation in methodologies, sample collection and timing of screening and inadequacies in the infrastructure for notification and continued care of identified patients. Of the many disorders of organic acid and fatty acid metabolism, a case can only be made for the introduction of newborn screening for glutaric aciduria type 1 (GA1; estimated incidence 1:40,000) and medium-chain acyl CoA dehydrogenase (MCAD) deficiency (estimated incidence 1:8000-1:15,000). Therapeutic advances for GA1 offer prevention of neurological damage but further investigation is required into the costs and benefits of screening for this disorder. MCAD deficiency is simply and cheaply treatable, preventing possible early death and neurological handicap. Neonatal screening for these diseases is dependent upon the introduction of tandem mass spectrometry (tandem MS). This screening could however also simultaneously detect some other commonly-encountered disorders of organic acid metabolism with a collective incidence of 1:15,000.(ABSTRACT TRUNCATED)

Cost-Benefit Analysis↗

Inhibition of pigeon breast muscle alpha-ketoglutarate dehydrogenase by structural analogs of alpha-ketoglutarate.

Inhibition of alpha-ketoglutarate dehydrogenase (KGD) by dicarboxylates with (oxaloacetate and ketomalonate) and without (malonate, succinate, and glutarate) alpha-keto group was studied. Ketodicarboxylates at low concentrations inhibit KGD in competitive manner. Increase in their concentrations results in appearance of the noncompetitive component. The extent of KGD inhibition by keto dicarboxylates increases with structural similarity of the inhibitor and the substrate, irrespective of preliminary incubation of the enzyme with the inhibitor. This is indicative of blocking the substrate-binding site of KGD by dicarboxylates. In contrast, inhibitory effect of dicarboxylates which contain no keto group increases as their structural similarity with the substrate decreases. Saturation of KGD with dicarboxylates of this type does not completely suppress the enzymatic activity. Alternatively, these analogs display competitive mode of inhibition. Analysis of the data obtained suggests that these dicarboxylates produce catalytically active triple complex keto substrate-KGD-dicarboxylate and that KGD which enters the composition of such a complex inhibits a decreased affinity for the keto substrate as a result of the inhibitor binding.

Animals↗

[Protein hydrolysis by immobilized enzymes].

The enzymic hydrolysis of some proteins (insulin-B-chain-S-sulfonate, S-aminoethylated lysozyme, bovine serum albumin) by immobilized peptidolytic enzymes is reported. Sepharose-bound pronase, trypsin and a protease from Thermoactinomyces sp. (MP), the latter both cross linked by glutaric dialdehyde and an exopeptidase mixture containing Sepharose-bound leucine aminopeptidase, carboxypeptidase A and a crude preparation of prolidase were used. After enzymic hydrolysis nearly all amino acids, except proline, were recovered in a 100% yield compared to the value of an acid reference hydrolysate. Tryptophan and methionine, which are partially destroyed by acid hydrolysis in the presence of oxygen could be recovered completely.

Aminopeptidases↗