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W de Vries

Publications and source records attributed to W de Vries.

At least 37 records · Page 2Linked to original sources

[Ascaris suum infection as a cause of clinical problems in cattle?].

A sudden decrease in milk yield, increased respiratory rate and occasional coughing were observed in dairy cows on two farms in spring 1991. Pigs were also kept on these farms, and pastures grazed by the cattle had been fertilised with pig slurry. Laboratory investigations of some of the cattle showed eosinophilia and high ELISA titres of antibodies against Ascaris suum. On one farm the clinical symptoms disappeared after the animals had been treated with oxfendazole and on the other farm the symptoms disappeared spontaneously with time.

Animals↗

Simultaneous flow cytometric detection of antibodies against platelets, granulocytes and lymphocytes.

We present a time-saving and objective flow cytometric immunofluorescence assay for the simultaneous detection of antibodies against platelets, granulocytes or lymphocytes using a reconstituted mixture of these cell populations. Platelets, granulocytes and lymphocytes could be distinguished on the basis of their forward (FSC) and sideways (SSC) light scattering properties plotted on scales of 4 log orders. After setting FSC/SSC gates around the platelets, granulocytes and lymphocytes, the reactivity of the sera with the cell populations was determined by histogram analyses of immunofluorescence for each gate. The flow cytometric assay of reconstituted cell mixtures showed a strong, positive correlation with a reference microscopic immunofluorescence assay of separate cell suspensions. The reproducible procedures for the isolation and staining of the cells and the electronic stability of the flow cytometer permitted the use of the same gate and marker settings throughout the experiments. Consequently, the entire analysis of data stored in list mode could be performed using a keystroke, so that time consuming and subjective manual analyses were avoided.

Antibodies↗

The effect of the dissolved oxygen concentration and anabolic limitations on the behaviour of Rhizobium ORS571 in chemostat cultures.

Chemostat cultures of Rhizobium ORS571 limited by the supply of oxygen or an anabolic substrate contained poly-beta-hydroxybutyrate (PHB). Low amounts of PHB (about 10%) were present in ammonia- or nitrate-limited cultures; higher amounts were found in Mg++-limited cultures (about 20%) and in oxygen-limited nitrogen-fixing cultures (37%). A method is described to calculate YATP values (g PHB-free biomass . mol-1 ATP) from the Ysucc values (g dry wt . mol-1 succinate) measured. Ysucc and YATP values in cultures limited by the supply of an anabolic substrate and in the oxygen-limited ammonia-assimilating culture were much lower than the values found in the PHB-free succinate-limited cultures. This shows that uncoupling of growth and energy production occurred. Therefore, H2/N2 ratio (mol hydrogen formed per mol nitrogen fixed) in nitrogen-fixing cultures could not be calculated from the comparison of the YATP value found in the nitrogen-fixing culture and the value found in the corresponding ammonia-assimilating culture. Although the optimal dissolved oxygen concentration (d.o.c.) for nitrogen-fixing cultures of Rhizobium ORS571 is 5 or 10 microM, nitrogen-fixing cultures could be obtained up to a d.o.c. of 40 microM. Not only nitrogenase but also hydrogenase was active at this d.o.c. However, accumulation of PHB (10%) may indicate that cultures grown at unfavourable oxygen concentrations (15-40 microM O2) were N-limited rather than energy-limited, which may be the result of partial inactivation or repression of nitrogenase at a higher d.o.c.

Adenosine Triphosphate↗

Localization of hydrogenase and nitrate reductase in Campylobacter sputorum subsp. bubulus.

Campylobacter sputorum subsp. bubulus contained hydrogenase activity after growth with lactate and nitrate and after growth with hydrogen and nitrate. After growth with hydrogen and nitrate a molar growth yield (g dry cells/mol hydrogen) of 5.6 was measured. Hydrogenase and nitrate reductase were membrane-bound enzymes. In cells with high hydrogenase activity the----H+/O,----H+/NO2- and----H+/NO3- values with hydrogen as the electron donor were 3.74, 2.61 and 4.36 respectively. In cells with low hydrogenase activity these values were 2.33, -0.86 and 1.31 respectively. These values and the stoichiometry of respiration-driven proton translocation (----H+/2e = 2) led to the conclusion that hydrogenase is located at the periplasmic side of the cytoplasmic membrane. In cells with low lactate dehydrogenase activity or low hydrogenase activity the reduction of nitrate to nitrite could be separated from the reduction of nitrite to ammonia. Positive----H+/NO3- values (between 0.9 and 1.7) with lactate or hydrogen as the electron donor were measured in these cells whereas----H+/ NO2- values were negative. From this result it was concluded that nitrate reductase is located at the cytoplasmic face of the cytoplasmic membrane. The results explain the previous observation that molar growth yields with nitrate were somewhat higher than those with nitrite.

Campylobacter↗

Hydrogen oxidation and nitrogen fixation in rhizobia, with special attention focused on strain ORS 571.

In this survey we describe the influence of hydrogen oxidation on the physiology of Rhizobium ORS 571. The presence of hydrogen is required for the synthesis of hydrogenase. Carbon substrates do not repress the synthesis of hydrogenase. The respiratory system contains cytrochromes of the b- and c-type. Cytochrome alpha 600 is present after growth at high oxygen tensions. The nature of the terminal oxidases functioning at low oxygen tensions has not been established yet----H+/O values with endogenous substrates are between 6 and 7. The results show the presence of two phosphorylation sites: site 1 (ATP/2e = 1.0) and site 2(ATP/2e = 1.33). By measuring molar growth yields it has been demonstrated that carbon-limited, nitrogen-fixing cultures obtain additional ATP from hydrogen oxidation, and that site 2 of oxidative phosphorylation is passed during hydrogen oxidation. A method is described to calculate ATP/N2 values (the total amount of ATP used by nitrogenase during the fixation of 1 mol N2) and H2/N2 ratios (mol hydrogen formed per mol N2 fixed) in aerobic organisms. For Rhizobium ORS 571 the ATP/N2 value is about 40 and the H2/N2 ratio is between 5 and 7.5. Cells obtained from oxygen-limited nitrogen-fixing cultures contain 30-40% poly-beta-hydroxybutyrate, which explains the high molar growth yields found. Hydrogen has not been detected in the effluent gas of these cultures, which may point to reoxidation of the hydrogen formed at nitrogen fixation. Calculations show that the effect of hydrogen reoxidation on the efficiency of nitrogen fixation (g N fixed X mol-1 substrate converted) is not very large and that the actual H2/N2 ratio is of much more importance. After addition of hydrogen to succinate-limited, ammonia-assimilating cultures, an initial increase of the Ysuccinate value (g dry wt X mol-1 succinate) is followed by a gradual decrease. This is accompanied by a large decrease of the YO2 value, and an increased permeability of the cytoplasmic membrane to protons. The results may be explained by a transition of the culture from an energy-limited state to a carbon-limited state.

Adenosine Triphosphate↗

Electron transport-linked proton translocation at nitrite reduction in Campylobacter sputorum subspecies bubulus.

Campylobacter sputorum subspecies bubulus contains a membrane-bound nitrite reductase which catalyses the six-electron reduction of nitrite to ammonia. Formate and L-lactate are used as hydrogen donors. Cells of C. sputorum grown with nitrate or nitrite contain cytochromes of the b- and c-type and a carbon monoxide-binding cytochrome c. In addition, a special membrane-bound carbon monoxide-binding pigment is found. Nitrite reduction with formate or L-lactate as a hydrogen donor is strongly inhibited by 2-n-heptyl-4-hydroxyquinoline-N-oxide (HQNO). Nitrite reduction by bacterial suspensions with lactate as a hydrogen donor is strongly inhibited by carbonylcyanide-m-chlorophenylhydrazone (CCCP) whereas nitrite reduction with formate as a hydrogen donor is not inhibited at all. Leads to H+/O values and leads to H+/NO-2 values were measured with ascorbate + N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD), formate (in the absence and presence of carbonic anhydrase) and L-lactate as a hydrogen donor. The results are summarized in a scheme for electron transport from formate or lactate to oxygen or nitrite which shows a periplasmic orientation of formate dehydrogenase and nitrite reductase and a cytoplasmic orientation of lactate dehydrogenase and oxygen reduction, and which shows proton translocation with a leads to H+/2e value of 2.0. The leads to H+/O and leads to H+/NO-2 values predicted by this scheme are in good agreement with the experimental values.

Campylobacter↗

Growth conditions and heat resistance of Citrobacter freundii.

The influence of the growth medium and the growth temperature on the heat resistance of Citrobacter freundii has been established. Logarithmic growth phase cells grown on rich media have a higher heat resistance than cells of the same phase grown on minimal media. This finding was independent of type of carbon source in the growth medium, but the kind of carbon source has a definite influence on the heat resistance. Logarithmic phase cells grown at 37 degrees C are much more heat stable than cells grown at 20 or 41 degrees C. Stationary growth phase cells are much more heat resistance than logarithmic phase cells, whereas Mg2+ - or glucose-starved cells are even slightly more heat stable than stationary phase cells.

Bacterial Proteins↗

Microaerophily.

Objections to previous definitions of "anaerobiosis" and "micro-aerophily" are discussed, and a new definition of "micro-aerophily" is proposed. A survey of physiological characteristics of the micro-aerophilic bacterium Campylobacter sputorum spp. bubulus is given, and the concept of "micro-aerophily" is illustrated by the results of a study on the oxygen metabolism and oxygen sensitivity of this bacterium.

Aerobiosis↗

Superoxide dismutase and hydrogen peroxide formation in Campylobacter sputorum subspecies bubulus.

Cell-free extracts of Campylobacter sputorum subspecies bubulus contained superoxide dismutase. The enzyme was located in the cytoplasmic fraction and insensitive to cyanide. After centrifuging a cell-free extract at 144000 x g for 1.5 h the total activity in the supernatant fraction was threefold higher than in the crude cell-free extract. The pellet fraction thus obtained was shown to have a lowering effect on superoxide dismutase activities from different sources in the assay method used here. C. sputorum responded to a raised oxygen tension in the culture by an increase in the superoxide dismutase activity. The ability to produce superoxide anion radicals (O2-.) during oxidation of formate and lactate was demonstrated. Furthermore C. sputorum was found to produce H2O2 while oxidizing formate. In experiments in which the reduction of cytochrome c by formate was followed, step-wise kinetics were observed. One of the steady states then obtained was attributed to the oxidizing action of H2O2, because it was abolished by the addition of catalase and lengthened by H2O2 added in addition to H2O2 formed as a product of formate oxidation. An overall reaction for formate oxidation by C. sputorum is discussed.

Campylobacter↗

ATP formation associated with fumarate and nitrate reduction in growing cultures of Veillonella alcalescens.

Molar growth yields, fermentation balances and enzyme activities were measured in Veillonella alcalescens grown anaerobically with different substrates in the absence or presence of fumarate or nitrate. The molar growth yields on malate (14.3 g dry wt bacteria/mole substrate) and citrate (19.3) were higher than that on lactate (8.6). The molar growth yield on lactate was increased to 15.5 or 19.8 by the addition of fumarate or nitrate, respectively, to the growth medium, and the molar growth yield on citrate was increased to 25.3 by addition of nitrate. Active growth on pyruvate was only observed in the presence of nitrate, and the molar growth yield was 25.5. From fermentation balances and fermentation systems similar YATP values (g dry wt bacteria/mole ATP) were calculated for all substrates or mixtures of substrates assuming that one mole of ATP is generated at the electron transport from pyruvate, NADH and NADPH to nitrate or fumarate whereas ATP is not produced in the electron transport from lactate to fumarate or nitrate, and, therefore, this assumption was considered to reflect the actual situation. The mean YATP value at a doubling time of 1 h was 16.5 g dry wt bacteria/mole ATP for growth without an added hydrogen acceptor, 14.4 for growth with fumarate, and 14.2 for growth with nitrate.

Adenosine Triphosphate↗

The effect of different dissolved oxygen tensions on growth and enzyme activities of Campylobacter sputorum subspecies bubulus.

Campylobacter sputorum subspecies bubulus was grown in batch cultures in which the dissolved oxygen tension (d.o.t) was maintained at various constant levels. At a range of d.o.t. from 0.002 to 0.05 atm, which allowed good growth (mean generation time approximately 1.5 h), L-lactate was preferentially consumed before D-lactate. L-lactate oxidation was accompanied by equimolar acetate production during exponential growth. A value for YL-lactate (g dry weight bacteria per mol L-lactate) of 54 was determined. Net acetate production stopped when C. sputorum started to use D-lactate after consumption of L-lactate. When a culture growing exponentially at the expense of L-lactate was shifted from a d.o.t. of 0.02 atm to a d.o.t. of 0.15 atm, growth was impaired, and L-lactate consumption and corresponding acetate production diminished. This decrease correlated with a loss of lactate dehydrogenase activity after the shift. Campylobacter sputorum appeared to possess cytochromes of the b- and c-type and a carbon monoxide-binding pigment. Evidence is given that the principal site of oxygen damage is lactate dehydrogenase rather than the cytochrome chain.

Acetates↗