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  • Blackwell Publishing Ltd  (2)
  • 1995-1999  (1)
  • 1985-1989  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 62 (1997), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The rigor mortis development of large Atlantic salmon was evaluated at a commercial plant using a sensory method, a mechanical rigorometer and low-frequency vibrations. The fish were classified according to rigor state using a neural network. Assessments were done with fish subjected to two different levels of handling stress prior to slaughter. White muscle high-energy phosphates and inosine monophosphate were used as indices of stress showing that handling stress may be considerable during commercial slaughter. Results indicate rigor assessment should be nondestructive and classificaton of rigor state was possible using a lowfrequency vibration method combined with a neural network.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The degradation of a panel of monoclonal antibodies (MoAb) bound to surface IgM (sIgM) was studied in three human Burkitt's lymphoma cell lines. The panel included MoAb that recognize several distinct epitopes associated with the F(cμ)5 domain, the cμ2 domain, and δ or λ light chains. The amount of degraded MoAb and the rate of their degradation varied considerably between the various antibodies. Properties of MoAb such as avidity or ability to cross-link sIgM did not significantly influence their degradation. The most consistent correlation between rate of degradation and MoAb used was the location of the epitope recognized by the individual MoAb. Thus, 7 out of 8 anti-light chain MoAb were degraded at a higher rate than 5 out of 5 anti-F(cμ)5 MoAb. One anti-cμ2 MoAb was degraded at a rate similar to the majority of anti-light chain MoAb. The intracellular transport of an anti-δ light chain MoAb and an anti-F(cμ)5 MoAb was studied in detail by subcellular fractionation in sucrose gradients. We found that the anti-δ light chain MoAb was transported more rapidly to lysosomes than the anti-F(cμ)5 MoAb, showing that they were sorted differently intracellularly.
    Type of Medium: Electronic Resource
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