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  • Articles: DFG German National Licenses  (14)
  • 1990-1994  (12)
  • 1965-1969  (2)
  • 11
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 46 (1990), S. 975-977 
    ISSN: 1420-9071
    Keywords: Marine alga ; agglutinin ; mitogen ; glycoprotein ; sugar-binding specificity ; biological activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A new agglutinin has been isolated from the red algaGracilaria bursa-pastoris by affinity chromatography on a yeast mannan-Cellulofine column. This agglutinin was isolated as a monomeric glycoprotein with a relatively low molecular weight. It had an isoelectric point of 4.7 and contained large amounts of Gly, Asx and Glx. It agglutinated trypsin-treated rabbit erythrocytes at the low concentration of 30 ng/ml. The activity was inhibited only by glycoproteins bearing N-glycans. This agglutinin also showed mitogenic activity for mouse splenic lymphocytes.
    Type of Medium: Electronic Resource
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  • 12
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have compared nucleotide sequences of the helper component-proteinase (HC-Pro) coding region of aphid transmissible (isolate 1) and non-transmissible (isolate 31) isolates of turnip mosaic virus (TuMV). HC-Pro coding regions of both TuMV isolates 1 and 31 were 1,374 nucleotide long. The nucleotide sequence homology between these isolates was 93.5%, with 89 nucleotides substitution. The nucleotides of HC-Pro regions of two isolates of TuMV genomes encoded 458 amino acids of Mr 51,746 (isolate 1) and Mr 51,764 (isolate 31). The deduced amino acid sequence homology between these isolates was 98.7% with six different amino acids. These amino acids appeared to regulate the activity of HC-Pro needed for aphid transmissibility of TuMV.
    Type of Medium: Electronic Resource
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  • 13
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Rat 3Y1 fibroblasts transformed by adenovirus type 12 or its E1A gene formed syncytia by cocultivation with Friend murine leukemia virus (MuLV)-producing cells. On the other hand, parental 3Y1 cells and those derivatives induced by other tumor viruses or chemical carcinogen showed no MuLV-mediated syncytium formation [N. Momozaki et al. (1990) Arch. Virol. 115: 123–126]. The expression of major histocompatibility complex (MHC) class I mRNA and antigens was significantly reduced in these Ad12- and E1A-transformed 3Y1 cells. In contrast, other tumor virus- and chemical carcinogen-transformed 3Y1 cells expressed MHC class I almost in normal levels as did parental 3Y1 cells. Furthermore, Ad12-transformed 3Y1 cells which started to express the transfected exogenous MHC class I gene,H-2L d, showed no more MuLV-mediated 3Y1 cell fusion. These results indicate that the expression of MHC class I on the cell membrane is closely related to the inhibition of 3Y1 cell fusion by MuLV.
    Type of Medium: Electronic Resource
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  • 14
    Electronic Resource
    Electronic Resource
    Springer
    Hydrobiologia 260-261 (1993), S. 589-593 
    ISSN: 1573-5117
    Keywords: lectins ; marine algae ; lectin detection ; biochemical properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lectins can be extracted more readily from marine algae if the plant material is freeze-dried or frozen in liquid nitrogen prior to homogenisation. The addition of detergents, such as Tween 80, to the extraction medium and diluents, enhances extraction and detection of the lectins. Marine algal lectins can be isolated by affinity chromatography using a general affinity complex such as yeast mannan-Cellulofine which facilitates the isolation of purified lectin for biochemical characterisation. Red algal lectins exist as three types: low molecular weight molecules which bind glycoproteins, but not monosaccharides and have no requirement for divalent cations; lectins which bind monosaccharides and related small molecules, but have no divalent cation requirements; larger lectins (M.W. 〉 64000) which bind monosaccharides in the presence of divalent cations. No green algal lectin characterised so far requires divalent cations for haemagglutination. Possibly, only green algal lectins capable of forming oligomers have the capacity to bind monosaccharides.
    Type of Medium: Electronic Resource
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