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  • 1975-1979  (5)
Collection
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 108 (1976), S. 279-286 
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. Ehrlich ascites tumour cells swollen in hypotonic medium reduce their volumes towards that found in isotonic medium. 2. This regulation of cell volume implies an adjustment of the intracellular amount of osmotically active substances, i.e. a type of “isosmotic intracellular regulation”. 3. Non-protein ninhydrin-positive substances were lost from the cells during this volume regulation. 4. Amino acid analyses show that the non-essential amino acids play a significant role in this process. 5. The relative decrease in concentration was larger for taurine than for any other measured inorganic and organic substance. The absolute change in intracellular taurine concentration is third only to changes in chloride and potassium. The role of taurine in osmoregulation is similar to that observed in many aquatic invertebrates. 6. The steady state distribution of amino acids varies with the magnitude of the Na+ and K+ concentration gradients between the cells and their environment. The ion gradient hypothesis fits our data only if we introduce a leakage pathway for the amino acids which is independent of the amino acid pump and which varies with the cell volume.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 87 (1976), S. 289-296 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The experiments show that abnormal proteins are degraded faster than normal ones in HeLa cells. Among the fragmentary proteins made in the presence of puromycin, those with low molecular weight are least stable. Proteins made after incubation with 5-fluorouracil or in the presence of some amino acid analogues are also unstable. Breakdown of proteins made in the presence or absence of puromycin is nearly unaffected by cycloheximide and is independent of pH between 7 and 8.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 92 (1977), S. 353-364 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Exponentially growing Balb/3T3 mouse fibroblasts contain protein populations with slow and fast turnover. These two stability classes were labelled selectively with 3H-leucine. The intracellular degradation of the proteins was then followed as the release into the medium of radioactive leucine.The degradation rate of both stability classes of protein is increased by about 55% in cultures whose growth is inhibited by high cell density. Serum-deprivation, which also halts cell growth, accelerates protein breakdown to a smaller extent, the increase for relatively stable and unstable proteins being 30% and 13%, respectively.The density-dependent increase in protein breakdown is also found in BHK21 cells but not in chick fibroblasts. Protein degradation in Balb/3T3 cells transformed by simian virus 40 is affected by serum-deprivation but not by cell density.The proteins which are relatively stable during growth were shown to become less stable in density-inhibited or serum-deprived cultures, and vice versa.Cycloheximide inhibits protein degradation to a variable extent. Dibutyryl adenosine-3′,5′-cyclic monophosphate has no effect on the protein degradation under the conditions investigated here.
    Additional Material: 4 Ill.
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  • 4
    Publication Date: 1977-09-01
    Print ISSN: 0021-9541
    Electronic ISSN: 1097-4652
    Topics: Biology , Medicine
    Published by Wiley
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  • 5
    Publication Date: 1976-03-01
    Print ISSN: 0021-9541
    Electronic ISSN: 1097-4652
    Topics: Biology , Medicine
    Published by Wiley
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