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  • 27.30+t  (2)
  • Cell fractionation  (2)
  • Springer  (4)
  • American Association for the Advancement of Science
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  • Springer  (4)
  • American Association for the Advancement of Science
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 170 (1976), S. 203-219 
    ISSN: 1432-0878
    Keywords: Exocrine pancreas ; Intracellular transport ; Cell fractionation ; Enzyme discharge
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The previous finding that intracellular transport of secretory proteins in the rat exocrine pancreas is accelerated by in vivo stimulation with a pancreatic secretagogue has been further analyzed. Using a radioassay for discharge of newly synthesized proteins, the rate of release was compared in control and prestimulated lobules. In control preparations discharge occurred with an initial lag period of 30 minutes and a maximum after two hours of incubation. After in vivo infusion of 5 × 10-8 g/hr. caerulein for 24 h in vitro discharge started after 10 minutes of in vitro incubation and attained a maximal rate after one hour. Using the same radioassay and several inhibitors of intracellular transport and granule discharge, it could be demonstrated that both processes were reduced to the same extent in controls and in lobules with accelerated transport. To obtain direct evidence for the degree of acceleration of the different transport steps between rough endoplasmic reticulum, Golgi complex and zymogen granules, the respective subcellular fractions of these organelles prepared and characterized ultrastructurally and biochemically. The rate of disappearance of newly formed proteins from rough microsomes and the appearance in smooth microsomes and zymogen granules were significantly increased after in vivo stimulation. The data substantiate an acceleration of the regular transport steps by the secretagogue. There was no indication that a high level of secretory activity leads to a rerouting of secretory proteins or to an omission of one of the regular steps in intracellular transport.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1434-601X
    Keywords: 27.30+t ; 21.10 Hw ; 21.60 Cs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Theγ-decays of levels in26Mg have been investigated up to 12.5 MeV excitation energy by proton-γ-ray coincidence measurements in the23Na(α, pγ) reaction at 14.2 and 16 MeV bombarding energy. Lifetime-measurements, made with the Doppler-shift attenuation method, and proton-γ-ray angular-correlation measurements were performed at Eα=14.2 MeV. Many high-spin states were observed, among them levels at 6,978 (5+), 7,283(4−), 7,395(5+), 7,953(5−), 8,202(6+), 8,472(6+), 9,065(5), 9,112(6+), 9,169(6−), 9,383 (6+), 9,542(5), 9,829(7+), 9,989(6+) and 12,479(8+, 7−) keV excitation energy. The spectrum of positive-parity states and their electromagnetic properties are reproduced with good accuracy by shell-model calculations which employ a unifieds-d shell Hamiltonian and the unrestricted configuration space of the 0d 5/2 1s 1/2 0d 3/2 shell. Members of five inferred rotational bands, withK π=0+, 2+, 3+, 0+ and 3− have been observed up to at leastI=6. TheK π=2+ band shows strong anomalies of excitation energies andE2 transition rates near theI=6 state. The static intrinsic quadrupole moments calculated from the shell model wave functions indicate transitions from prolate to oblate deformation within theK π=2+ band and also the ground state band. The lowest lyingI π=4+ state appears to be “spherical” and cannot be associated with a rotational band.
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  • 3
    ISSN: 1434-601X
    Keywords: 27.30+t ; 21.10 Hw ; 21.60 Cs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract New shell model calculations have predicted several high-spin (I π=5+ and 6+) levels in28Si near 10 MeV excitation energy which are missing from or ambiguous in existing experimental studies. Angular distributions, linear polarizations and Doppler-shifts ofγ-rays have been measured for theγ-decay of theE p=1,911 and 2,073 KeV resonances of the27Al(p, γ) reaction in an attempt to discover these missing states or confirm the discrepancies between experiment and theory. The excitation energies and spin-parities of the resonances were determined as 13,424.4±0.2 keV,I π=5+ and 13,582.3±0.5 keV,I π=6+. States populated in theγ-decay of these resonances were assigned spins and parities as follows: 11,777 keV,I π=5+; 11,331 keV,I π=6+; 10,417 keV,I π=5+; 9,417 keV,I π=4+ and 8,945 keV,I π=5+. On the basis ofγ-ray transition rates T=1 is assigned to the 13,424 keV level and T=0 to the 10,417 and 11,777 keV levels. With the new data excellent agreement is achieved between the experimental spectrum of28Si and the new shell model predictions. These data provide evidence for aK π=3+ rotational band comprised by the 6,276, 6,889, 8,945 and 11,331 keV levels. This band emerges also from the shell model wave functions as do theK π=0+ bands based on the ground state and the 6,691 keV state.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 193 (1978), S. 93-105 
    ISSN: 1432-0878
    Keywords: Exocrine pancreas ; Cell fractionation ; Glycoproteins ; Membrane proteins ; Intracellular transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The transcellular movement of fucosylated glycoproteins has been studied in vitro using rat pancreatic lobules and cell fractionation procedures, and has been compared with the well established pathway of secretory proteins. Using tritiated leucine as pulse label for the latter, their translocation from the rough endoplasmatic reticulum into the Golgi complex and finally into zymogen granules could be followed. In the case of glycoproteins, 14C-fucose was incorporated mainly into the smooth microsomal fraction (representative of the Golgi complex) and only one third of this specific activity was transported into the zymogen granule fraction. A detailed analysis of this fraction after separation of the content of zymogen granules from their membranes revealed a predominant labeling of membrane glycoproteins by 14C-fucose. In comparison, leucine-labeled bulk proteins were found almost exclusively in the zymogen granule content fraction, with little radioactivity in the membrane fraction. The data indicate a concomitant synthesis of fucosylated glycoproteins destined in part for the zymogen granule membrane and to a greater amount associated with the smooth microsomal fraction. The results are discussed in the light of recent findings indicating that about 40% of the proteins in the zymogen granule membrane are made up of one major glycoprotein which could be involved in the mechanism of exocytosis.
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