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  • 1
    Electronic Resource
    Electronic Resource
    Buckling and cracking of thin films on compliant substrates under compression (2000)
    Springer
    International journal of fracture 104 (2000), S. 169-179 
    Details
    ISSN: 1573-2673
    Keywords: Thin film ; delamination ; buckling ; cracking ; compliant substrate.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract It is shown that unless the substrate is at least as stiff as the film, the energy stored in the substrate contributes significantly to the energy release rate of film delamination under compression either with or without cracking. For very compliant substrates, such as polyethylene terephthalate (PET) with a indium tin oxide (ITO) film, the energy release rate allowing for the deformation of the substrate can be more than an order of magnitude greater than the value obtained neglecting the substrate's deformation. The argument that buckling delaminations tunnel at the tip rather than spread sideways because of increase in mode-mixity may need modification; it is still true for stiff substrates, but for compliant substrates the average energy release rate decreases with delamination width and the limitation in buckled width may be due to this stability as much as the increase in mode-mixity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007628800620
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of Oxodiperoxovanadate (V) Complexes on the Activity of Green Crab (Scylla serrata) Alkaline Phosphatase (2000)
    Springer
    Biochemistry (Moscow) 65 (2000), S. 1424-1428 
    Details
    ISSN: 1608-3040
    Keywords: alkaline phosphatase ; oxodiperoxovanadate ; inhibition ; inactivation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme that catalyzes the nonspecific hydrolysis of phosphate monoesters. The effects of some pollutants in seawater on the activity of the enzyme will result in the loss of the biological function of the enzyme, which will affect the exuviating crab shell and threaten the survival of the animal. In the present paper, the effects of four oxodiperoxovanadate (V) complexes on the activity of green crab alkaline phosphatase have been studied. The results show that these vanadate derivatives can lead to reversible inactivation. The equilibrium constants for binding of inhibitors with the enzyme and/or the enzyme–substrate complexes have been determined. The results show that sodium (2,2'-bipyridine)oxodiperoxovanadate, pV(bipy), and potassium oxodiperoxo-(1,10-phenanthroline)vanadate, pV(phen), are competitive inhibitors, while potassium picolinato-oxodiperoxo-vanadate, pV(pic), and oxalato-oxodiperoxovanadate, pV(ox), are mixed-type inhibitors. These results suggest that pV(bipy) is a considerably more potent competitive inhibitor than pV(phen) and that the competitive inhibition effect of pV(pic) is stronger than that of pV(ox), but the non-competitive inhibition effect of pV(ox) is stronger than that of pV(pic).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1002813125201
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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