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Digitale Medien

Pairing properties of nuclear matter at finite temperature (1989)

Kucharek, H. ; Ring, P. ; Schuck, P.

Springer

The European physical journal 334 (1989), S. 119-124

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ISSN: 1434-601X

Schlagwort(e): 21.10.−k ; 21.65.+f ; 21.30.+y

Quelle: Springer Online Journal Archives 1860-2000

Thema: Physik

Notizen: Abstract The Gogny effective interaction is used to calculate the pairing properties of symmetric nuclear matter at various densities and temperatures. A pairing collapse is predicted at a critical temperature of half the gap parameter at temperature zero. The phase diagram which separates normal and superfluid phases is calculated.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01294212

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Digitale Medien

Localization of the incorporation of 3H-galactose and 3H-sialic acid into thyroglobulin in relation to the block of intracellular transport induced by monensin (1987)

Ring, P. ; Björkman, U. ; Ekholm, R.

Springer

Cell & tissue research 250 (1987), S. 149-156

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ISSN: 1432-0878

Schlagwort(e): Thyroid gland (porcine) ; Thyroglobulin ; 3H-Galactose ; Sialic acid ; Monensin ; Intracellular transport ; Secretion

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Summary The Na+/K+ ionophore monensin is known to arrest the intracellular transport of newly synthesized proteins in the Golgi complex. In the present investigation the effect of monensin on the secretion of 3H-galactose-labeled and 3H-sialic acid-labeled thyroglobulin was studied in open thyroid follicles isolated from porcine thyroid tissue. Follicles were incubated with 3H-galactose at 20° C for 1 h; at this temperature the labeled thyroglobulin remains in the labeling compartment (Ring et al. 1987a). The follicles were then chased at 37° C for 1 h in the absence or presence of 1 μM monensin. Without monensin substantial amounts of labeled thyroglobulin were secreted into the medium, whereas in the presence of the ionophore secretion was inhibited by 80%. Since we have previously shown (Ring et al. 1987 b) that monensin does not inhibit secretion of thyroglobulin present on the distal side of the monensin block we conclude that galactose is incorporated into thyroglobulin on the proximal side of this block. Secretion was also measured in follicles continuously incubated with 3H-galactose for 1 h at 37° C in the absence or presence of monensin. In these experiments secretion of labeled thyroglobulin was inhibited by about 85% in the presence of monensin. Identically designed experiments with 3H-N-acetylmannosamine, a precursor of sialic acid, gave similar results, i.e., almost complete inhibition of secretion of labeled thyroglobulin in the presence of monensin. The agreement between the results of the galactose and sialic acid experiments indicates that sialic acid, like galactose, is incorporated into thyroglobulin on the proximal side of the monensin block. Considering observations made in other cell systems the present results suggest that galactosylation and sialylation of thyroglobulin are completed within the Golgi complex.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00214666

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Digitale Medien

The effect of monensin on thyroglobulin secretion (1987)

Ring, P. ; Björkman, U. ; Johanson, V. ; [weitere]

Springer

Cell & tissue research 248 (1987), S. 153-160

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ISSN: 1432-0878

Schlagwort(e): Thyroid gland ; Thyroglobulin ; Intracellular transport ; Secretion ; Monensin ; Isolated follicles ; Pig

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Summary The effect of monensin on the secretion of thyroglobulin was studied in open follicles isolated from pig thyroid tissue; in this system, thyroglobulin is secreted into the incubation medium. When monensin was present during a 4-h chase incubation after pulse-labelling with3H-leucine, the secretion of labelled thyroglobulin was reduced by about 85%; in electron-microscopic autoradiographs of rat thyroid lobes labelled and chase-incubated under similar conditions the relative number of grains over follicle lumina was strongly reduced when monensin was present during the chase. These observations are in agreement with the consensus that monensin arrests transport of secretory proteins in the Golgi complex. In other experiments, pulse-labelled follicles were chase-incubated for 1.5 h whereby labelled thyroglobulin was transported from the RER to exocytic vesicles. Monensin present during a subsequent chase of 0.5 h caused only a moderate decrease of labelled thyroglobulin secretion. TSH present during the second chase-stimulated secretion in both control and monensin-exposed follicles. TSH also caused a drastic reduction of exocytic vesicles in rat thyroid lobes, and the number of vesicles remaining in the cells was the same in controls and lobes exposed to the ionophore. The observations are interpreted to show that monensin does not inhibit the basal or TSH-stimulated transport of thyroglobulin from the site of monensin-induced arrest in the Golgi complex to the apical cell surface or the exocytosis of thyroglobulin.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01239976

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