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Biomedical subjects

H Degn

Publications and source records attributed to H Degn.

At least 37 records · Page 2Linked to original sources
PubMed1980

Transcutaneous oxygen measurement during thoracic anaesthesia.

The value of transcutaneous oxygen tension (tcPO2) as an oxygen parameter during uncomplicated thoracic anaesthesia was examined in ten patients anaesthetized with oxygen-nitrous oxide and enflurane or flunitrazepam/fentanyl. tcPO2 was measured with the Radiometer TCM-I monitor at 45 degrees C. Measuring interference due to the anaesthetic agents was not observed. tcPO2 was found to be lower than the arterial tension (PaO2) at any inspiratory oxygen fraction (FIO2). When the peroperative readings were related to the preoperative values, no statistically significant difference was found between PaO2 and tcPO2 at FIO2 - 0.5, 0.4 and 0.3 (P greater than 0.3). Linear regression between PaO2 and tcPO2 shows disparity in pre- and peroperative regression. tcPO2 (preoperative) = -2.2 + 1.03 X PaO2 (4 = 0.89) tcPO2 (preoperative) = +3.1 + 0.56 X PaO2 (r = 0.87). This disparity indicates a decrease in the tcPO2/PaO2 ratio with increasing PaO2. It is concluded that tcPO2 cannot substitute for PaO2, but tcPO2 and PaO2 proved to be equally useful as oxygen parameters in the examined patients. Interpretation of tcPO2 during anaesthesia, however, necessitates a preoperative measurement as reference.

Adult↗
PubMed1979

The effect of inhibitors on the oxygen kinetics of terminal oxidases of Acanthamoeba castellanii.

1. Respiration of growing cultures of Acanthamoeba castellanii is inhibited less than 60% by azide (35 mM); the respiration of early-exponential-phase cultures differs from that of late-exponential-phase cultures in being stimulated by up to 120% by low concentrations (less than 1 mM) of this inhibitor. Azide (0.5 mM) plus 1 mM-salicylhydroxamic acid gives 80% inhibition of respiration in early- or late-exponential-phase cultures. 2. Lineweaver-Burk plots of 1/v against 1/[O2] for growing and stationary-phase cultures give values of less than 1 muM for the apparent Km for oxygen. 3. These values are not significantly altered when determined in the presence of 1 mM-salicylhydroxamic acid. 4. Higher values (greater than 7 muM) for apparent Km values for oxygen were obtained in the presence of azide, which gives non-linear Lineweaver-Burk plots. 5. Competitive inhibition of respiration by CO occurs with Ki 2.4 muM. 6. The results are discussed in terms of the presence of three terminal oxidases in this organism, namely two oxidases with high affinities for oxygen (cytochrome c oxidase of the main phosphorylating electron-transport chain and the salicylhydroxamic acid-sensitive oxidase) and a third oxidase with a low affinity for oxygen, sensitive to inhibition by cyanide but not by azide or salicylhydroxamic acid. The relative contributions to oxygen utilization by these oxidases change during the growth of a batch culture.

Amoeba↗
PubMed1978

Steady-state kinetics of laccasse from Rhus vernicifera.

The steady-state kinetics of laccasse (monophenol, dihydroxyphenylalanine: oxygen oxidoreductase, EC 1.14.18.1) from the lacquer tree Rhus vernicifera is investigated using the respirograph method to produce Lineweaver-Burk plots of oxygen consumption rate against oxygen concentration. A ping-pong mechanisms is established. The kinetic constants obtained according to the model is in close agreement with the corresponding values obtained from earlier studies on the transient reactions between the reduced enzyme and oxygen (Andréasson, L.E., Brändén, R. and Reinhammar, B. (1976) Biochim. Biophys. Acta 438, 370--379) and between the oxidized enzyme and reducing substrates (Andréasson, L.E. and Reinhammar, B. (1976) Biochim. Biophys. Acta 445, 579--597).

Catechol Oxidase↗
PubMed1978

Oscillatory kinetics of the peroxidase-oxidase reaction in an open system. Experimental and theoretical studies.

1. The oscillations in the peroxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7)-catalyzed reaction between NADH and O2 are undamped when the reaction is carried out in a system open to both substrates and when 2,4-dichlorophenol and methylene blue are present in the solution. 2. The waveform of the oscillations changes when the concentration of peroxidase is varied. 3. The waveforms obtained experimentally can be simulated by a branched chain reaction model in which the branching is quadratic. 4. A correlation between the present knowledge of the reaction and the model can be made by combining well established and hypothetical reaction steps into a few reaction schemes. A selection among schemes however, is not possible at the present time. 5. Compound III participates in the reaction as an active intermediate. This is possible because dichlorophenol stimulates the break down of compound III.

Computers↗
PubMed1977

Chaos in an enzyme reaction.

Dynamic systems are usually thought to have either monotonic or periodic behaviour. Although the possibility of other types of behaviour has been recognised for many years, the existence of non-monotonic, non-periodic behaviour in dynamic systems has been firmly established only recently. It is termed chaotic behaviour. A review on the rapidly expanding literature on chaos in discrete model systems described by difference equations has been published by May. Rössler, on the other hand, has discussed a few published works on systems of differential equations with chaotic solutions, and he has proposed a three-component chemical model system which he argues has chaotic solutions [figure see text]. The argument is based on a theorem by Li and Yorke. Here we report the finding of chaotic behaviour as an experimental result in an enzyme system (peroxidase). Like Rössler we base our identification of chaos on the theorem by Li and Yorke.

Catalysis↗
PubMed1977

Steady-state oxygen kinetics of terminal oxidases in Trypanosoma mega.

Steady-state oxygen kinetics of Trypanosoma mega reveal the presence of 3 oxidases. These include an oxidase which is sensitive to salicylhydroxamic acid (SHAM) but insensitive to sodium azide. This oxidase could be the L-alpha glycerophosphate oxidase present in bloodstream trypanosomes. In addition, and oxidase is present wthich is azide-sensitive but SHAM-insensitive. This oxidase is inhibited by CO and is probably cytochrome aa3. A 3rd oxidase is insensitive to both azide and SHAM but is inhibited by CO and is possibly cytochrome o. Reciprocal plots of T. mega reveal the presence of 2 oxidases that are inhibited by CO. These results are discussed in the light of previous evidence suggesting the presence of several oxidases and a branched electron transport system in T. mega.

Animals↗
PubMed1976

The effect of oxygen concentration on the steady-state kinetics of the solubilized cytochrome c oxidase.

1. The steady-state kinetics of ascorbate oxidation as a function of oxygen concentration was measured with a solubilized cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) preparation. 2. Linear double reciprocal plots were obtained at various fixed concentrations of ascrobate, cytochrome c and cytochrome aa3. 3. The results are interpreted in terms of an oxidase model similar to that put forward by Minnaert in 1961 (Minnaert, K. (1961) Biochim. Biophys. Acta 50, 23-34). 4. The Km for oxygen at infinite cytochrome c concentration is 0.95 muM and the intramolecular rate constant for the transfer of electrons from cytochrome c to cytochome aa3 is 400 s(-1). According to the model, this implies that the second order rate constant for the reaction between oxygen and the oxidase is 9.5 X 10(7)M(-1)-s(-1).

Animals↗
PubMed1974

The effect of energization on the apparent Michaelis-Mentne constant for oxygen in mitochondrial respiration.

Lineweaver-Burk plots of 1/v against 1/[O(2)] for rat liver mitochondrial respiration with succinate or ascorbate+NNN'N'-tetramethyl-p-phenylenediamine as substrates are non-linear. In state 3u (uncoupled by trifluoromethoxycarbonyl cyanide phenylhydrazone) such plots tend to be concave upward, whereas in state 4 (energized) the plots were concave downward. The apparent K(m) for oxygen is larger in state 4 than in state 3u, despite the higher turnover in the latter system. It is postulated that at least one reversible reaction occurs between cytochrome c and cytochrome c oxidase, whose rate is increased on energization (reversed electron transfer); a model including such a reaction is proposed which accounts semiquantitatively for the observations.

Animals↗
PubMed1973

The occurrence of a stepwise-decreasing respiration rate during oxidative assimilation of different substrates by resting Klebsiella aerogenes in a system open to oxygen.

The addition of an oxidizable substrate to a continuous culture of Klebsiella aerogenes is known to cause an increased respiration rate that decreases in discrete steps as the added substrate is being exhausted. We have used a simple new technique to show that this phenomenon is also produced by washed, resting cells harvested from batch or continuous growth culture. The stepwise-decreasing respiration rate is caused by the exhaustion of different pools of intermediates. Each plateau of respiration rate is a measure of the activity of one or more enzymes that are rate limiting in the exhaustion of pools of intermediates. If the identities of the enzymes that are rate limiting at the different plateaux are known, the method may allow the determination, in one experiment, of the activities of up to six different enzymes in the intact bacteria. Integration of the respiration-rate measurements yields the total amount of O(2) taken up. After the addition of glucose to the washed resting bacteria 37% of the amount of O(2) required for the complete oxidation of the glucose was taken up. Acetate, pyruvate and succinate were all oxidized to the extent of 51%.

Acetates↗