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Biomedical subjects

O Hansen

Publications and source records attributed to O Hansen.

At least 163 records · Page 9Linked to original sources
PubMed1979

Facilitation of ouabain binding to (Na+ + K+)-ATPase by vanadate at in vivo concentrations.

In the presence of Mg2+ vanadate was shown to facilitate ouabain binding to (Na+ + K+)-ATPase in much the same way as Pi does. Thus the hypothesis that vanadate interacts with the phosphate site of the enzyme seems to be supported by ouabain binding experiments. At given ouabain concentrations maximum binding is achieved at microM concentrations of vanadate whereas mM concentrations of Pi are needed. Na+ as well as K+ counteract ouabain binding but some cardiac glycoside binding is still possible at in vivo concentrations of these cations. A minor contamination of the enzyme preparations with vanadate could explain the in vitro binding of ouabain that can be obtained with Mg2+ and in the absence of Pi.

Kinetics↗
PubMed1978

The effect of sodium on inorganic phosphate- and p-nitrophenyl phosphate-facilitated ouabain binding to (Na+ + K+)-activated ATPase.

The effect of the hydrolysis product Pi and the artificial substrate p-nitrophenyl phosphate (p-nitrophenyl-P) on ouabain binding to (Na+ + K+)-activated ATPase was investigated. The hypothesis that (Mg2+ + p-nitrophenyl-P)-supported ouabain binding might be due to Pi release and thus (Mg2+ + Pi)-supported could not be confirmed. The enzyme . ouabain complexes obtained with different substrates were characterized according to their dissociation rates after removal of the ligands facilitating binding. The character of the enzyme . ouabain complex is determined primarily by the monovalent ion present during ouabain binding, but, qualitatively at least, it is immaterial whether binding was obtained with p-nitrophenyl phosphate or Pi. The presence or absence of Na+ during binding has a special influence upon the character of the enzyme . ouabian complex. Without Na+ and in the presence of Tris ions the complex obtained with (Mg2+ + Pi) and that obtained with (Mg2+ + p-nitrophenyl-P) behaved in a nearly identical manner, both exhibiting a slow decay. High Na+ concentration diminished the level of Pi-supported ouabain binding, having almost no effect on p-nitrophenyl phosphate-supported binding. Both enzyme . ouabain complexes, however, now resembled the form obtained with (Na+ + ATP), as judged from their dissociation rates and the K+ sensitivity of their decay. The complexes obtained at a high Na+ concentration underwent a very fast decay which could be slowed considerably after adding a low concentration of K+ to the resuspension medium. The most stable enzyme . ouabain complex was obtained in the presence of Tris ions only, irrespective of whether p-nitrophenyl phosphate of Pi facilitated complex formation. The presence of K+ gave rise to a complex whose dissociation rate was intermediate between those of the complexes obtained in the presence of Tris and a high Na+ concentration. It is proposed that the different ouabain dissociation rates reflect different reactive states of the enzyme. The resemblance between the observations obtained in phosphorylation and ouabain binding experiments is pointed out.

Adenosine Triphosphatases↗
PubMed1978

Flow requirements in the Hafnia modifications of the Mapleson circuits during spontaneous respiration.

The Mapleson A, B, C and D circuits can be changed into non-polluting circuits by employing continuous gas evacuation directly from the circuit, via an ejector flowmeter (Jørgensen 1974); Mapleson A and C circuits with this modification have been described previously as the Hafnia A and C circuits (Christensen 1976, Thomsen & Jørgensen 1976). If evacuation from a closed reservoir is employed, total removal of the expired and surplus gases from the operating theatre is obtained (Jørgensen & Thomsen 1976). There will be resistance to expiration in all the circuits with a relief valve for the discharge of surplus gas. If surplus gas is continuously removed directly from the anaesthetic circuit, the patient breathes in an air compartment at ambient pressure, as long as the removal rate equals the inflow of fresh gas. The relief valve is only included in the circuit to ensure that high pressures do not develop. As in any other circuit, the relief valve remains open except during controlled ventilation. A dumping valve may also be included as a safeguard against low pressures (Jørgensen & Thomsen 1976). The flow requirements of the Hafnia B and D circuits and the corresponding Mapleson circuits have been studied in conscious, spontaneously breathing subjects, and the results are discussed in relation to the flow requirements of other semi-closed system.

Anesthesia, Inhalation↗
PubMed1977

Active Na-K transport and the rate of ouabain binding. The effect of insulin and other stimuli on skeletal muscle and adipocytes.

1. The effect of stimulation or inhibition of active Na-K transport on [(3)H]ouabain binding has been investigated in isolated soleus muscles and adipocytes.2. In rat soleus muscle, the ouabain-sensitive component of (42)K influx was stimulated by insulin (100 m-u/ml.), adrenaline (6 x 10(-6)M), and by pre-incubation with veratrine (10(-5)M) or in a K-free buffer. In all of these instances, the rate of ouabain binding was increased by 41-113%. Conversely, pre-treatment with tetracaine (0.2 mM) decreased the (42)K-influx and diminished the rate of [(3)H]ouabain binding by 36%.3. Neither insulin, adrenaline or tetracaine produced any detectable change in the total number of ouabain-binding sites (as measured under equilibrium conditions) in rat soleus muscle.4. In mouse and guinea-pig soleus muscle and in fat cells isolated from rats, insulin also increased the rate of [(3)H]ouabain binding without producing any significant change in the total number of ouabain-binding sites.5. Both in soleus muscle and the epididymal fat pad of the rat, there was a linear correlation between (42)K influx and the initial rate of [(3)H]ouabain binding.6. It is concluded that the rate of ouabain binding is determined significantly by the rate of active Na-K transport, but within the time intervals studied (4-6 hr) stimulation or inhibition of the Na pump does not lead to any appreciable change in the total number of Na pumps. It seems unlikely that the stimulation of active Na-K transport by insulin or adrenaline is due to unmasking or de novo synthesis of Na pumps.

Adipose Tissue↗