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  • 1990-1994  (1)
  • 1980-1984  (1)
  • 1970-1974
  • 1965-1969
  • Glycosylation  (1)
  • Locomotion  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Increased fructose-lysine of nail protein in diabetic patients (1984)
    Springer
    Journal of molecular medicine 62 (1984), S. 477-478 
    Details
    ISSN: 1432-1440
    Keywords: Fructose-lysine ; Furosine ; Haemoglobin A1 ; Glycosylation ; Diabetes mellitus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Fructose-lysine, which is formed by binding glucose to lysine, is degraded on acid hydrolysis into furosine. Furosine was determined by high-performance liquid chromatography according to the method of Schleicher et al. Furosine values were significantly higher in diabetic patients than in healthy subjects, and significantly correlated with haemoglobin A1 (HbA1) values. These results suggest that furosine, like HbA1, may become an indicator of long-term blood glucose control in diabetic patients and be useful in investigating diabetic complications on the level of tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01726910
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Calcium control of actin-myosin-based contraction in Triton-treated murine bladder tumor cells (1993)
    Springer
    Urological research 21 (1993), S. 429-433 
    Details
    ISSN: 1434-0879
    Keywords: Actin ; Calcium ion ; Contraction ; Locomotion ; Murine bladder tumor cells ; Myosin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using mouse bladder tumor cells (MBT-2 cells) and epithelial cells, the present study evaluated the functional characteristics of the actomyosin system in bladder cancer cells. An immunofluorescence study demonstrated the presence of contractile proteins (actin and myosin) in MBT-2 cells as well as bladder epithelial cells. Triton-treated MBT-2 cells and epithelial cells showed a Ca2+-dependent contraction. This was inhibited by N-ethylmaleimide-modified myosin subfragment 1 (NEM-S1), demonstrating that the interaction between actin and myosin is responsible for the contraction of Triton-treated cells. The extent of Ca2+-dependent contraction was much greater in MBT-2 cells than in epithelial cells. These results suggest that MBT-2 cells possess a locomotive apparatus consisting of actin and myosin, and that Ca2+ can activate this actomyosin system, leading to the contraction or active locomotory movement of tumor cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00300081
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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