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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 15 (1988), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Murine splenocytes which contained B cells activated by in vivo exposure to affinity-purified goat anti-mouse IgD (GaMD) antibody were utilized to present major histocompatibility complex (MHC) and non-MHC minor lymphocyte-stimulating (Mlsa) determinants in a primary mixed lymphocyte reaction (MLR). As the time in hours after in vivo exposure to GaMD increased, splenocytes from adult mice showed a co-ordinate increase in cell size, expression of public and private MHC class II antigenic determinants and MHC and Mlsa antigen-presenting capacity. This augmented alloantigen-presenting capacity was demonstrable with either irradiated or mitomycin C-treated adult splenocytes. In contrast, GaMD-treated neonatal splenocytes from 10-day-old mice demonstrated no significantly increased class II expression or enhanced MHC stimulatory capacity, but nevertheless triggered augmented responder cell proliferation across an Mlsa barrier. Thus, increased class II expression or presenting capacity may not be required for an augmentation in splenocyte Mls-stimulating ability to occur. In vitro exposure of T cell-depleted splenocytes or highly purified small resting B cells to GaMD or lipopolysaccharide (LPS) induced a substantially increased ability in those populations to present MHC and Mlsa antigens in a primary MLR. Hence in vivo or in vitro activation of B lymphocytes in a stimulator cell population may yield more effective presentation of MHC and non-MHC determinants.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), 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: Studies were carried out to determine the protein quality of whole dried honey bees (56.8% crude protein, 11.1% chitin) and honey bee protein concentrate (64.2% crude protein, 0% chitin). The levels of most of the indispensable amino acids were higher in honey bee protein concentrate than in whole dried bees. The true protein digestibility was higher (P 〈 0.05) in the concentrate (94.3%) than in whole dried honey bees (71.5%), as were the amino acid availabilities. PER and NPU were 2.47 and 62, respectively, in the concentrate and 1.50 and 42.5, respectively, in whole dried honey bees. The removal of chitin following alkali extraction of whole dried honey bees is primarily responsible for the improvement in protein quality.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 522 (1988), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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