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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 204 (1995), S. 229-243 
    ISSN: 1432-041X
    Keywords: Glycan structures ; Lectins ; Drosophila Embryogenesis ; Development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The spectrum of lectin binding sites as it emerges during embryonic development of Drosophila was analysed by means of fluorescein-labelled lectins. As development and morphogenesis proceed, the reaction pattern becomes more and more complex. Mannose/glucose-, mannose-, N-acetylglucosamine- and poly-N-ace-tylglucosamine-specific lectins bind ubiquitously. Nuclear envelopes only have binding sites for wheat germ agglutinin. N-acetylgalactosamine-binding lectins are specific for ectodermal derivatives. Gaβ-3-N-acetylgalac-tosamine-binding lectins are highly selective markers for neural structures, haemocytes and Garland cells. It is also shown that Drosophila laminin is differentially glycosylated. The possible implications of differential and germ layer-specific glycosylation are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1638-1640 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The A4 isoform of the bark lectin RPbAI from Robinia pseudoacacia has been crystallized in two different crystal forms. Crystal form I grows in the P21 space group with two tetramers in the asymmetric unit, whereas crystal form II grows in the I222 space group with a monomer in the asymmetric unit. Data sets were collected for both crystal forms to resolution limits of 2.55 and 1.81 Å, respectively, which will allow successful structure determinations.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 609-611 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: MornigaM, a lectin from Morus nigra, belongs to the mannose-binding subgroup of the family of jacalin-related plant lectins. It was crystallized in the P65 space group, with unit-cell parameters a = b = 110.74, c = 159.28 Å. The partially merohedrally twinned crystals could be detwinned and a subsequent molecular-replacement solution could be found using the coordinates of jacalin. Preliminary analysis clearly shows the tetrameric assembly of this protein. Furthermore, data from MornigaM crystals soaked in a mannose solution were collected.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals have been grown of a mannose-specific lectin from bluebell (Scilla campanulata) bulbs in a form suitable for X-ray diffraction studies. The crystals, which diffract to high resolution, grew in hanging drops by vapour diffusion, equilibrating with a solution of 70% saturated ammonium sulfate at pH 4.7–4.8 at 293 K, in the absence of any mannose saccharides. Crystals are orthorhombic, P21212, with unit-cell dimensions a = 70.78, b = 93.69, c = 46.92 Å. The functional lectin molecule is organized as a tetramer of four identical 14 kDa subunits, with only two subunits in the asymmetric unit. Data to 1.86 Å resolution have been recorded and the structure determined by the molecular replacement method.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 220-221 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A mannose-specific lectin from Calystegia sepium has been crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The needle-shaped crystals are orthorhombic, space group C2221 with cell dimensions a = 55.2(1), b = 55.9 (1), c = 196.1 (1) Å. Fresh crystals diffract to 1.9 Å resolution on a synchrotron radiation source. The asymmetric unit contains a dimer of two identical 16 kDa subunits with a packing density of 2.36 Å3 Da−1. Intensity data have been observed beyond 2.0 Å, but reasonable statistics restricted the usable range to 2.0 Å.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant breeding 98 (1987), S. 0 
    ISSN: 1439-0523
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Wheat germ agglutin (WGA) present in the embryo of a bread wheat grain is a mixture of three isolectins, viz CLA, CLB and CLD which are coded by genes located on die chromosomes 1A, 1B and 1D. Their respective absolute amounts were determined in 62 Nigerian and five Chad landraces. Added was the Madagascar variety ‘Kanem’ which is stated to be selected from Chad material. Some of the Nigerian landraces were formerly identified as derived from Indian Pakistani wheat varieties/landraces introduced into Northern Nigeria before 1940. These had relatively high CLD/GLA and CLB/CLA ratios. Other Nigerian landraces with such high ratios were postulated to come from India/Pakistan, too.The Chad wheats, except ‘Kanem’, have WGA amounts and-ratios similar to those native to Northern Nigeria. This may point to a common history. ‘Kanem’ is said to be bred in Madagascar from Chad wheats. Apparently it has a different origin.So the determination of the WGA amount and its isolectin composition is a helpful means to identify the history of a land race or of an improved variety.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0167-0115
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Experimental dermatology 10 (2001), S. 0 
    ISSN: 1600-0625
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Changes in carbohydrate residue expression and in proteoglycan distribution occur during different stages of tumor development and progression. However, few data concerning carbohydrate residue analysis as performed by lectin histochemistry and proteoglycan distribution of Merkel cell carcinoma, a rare malignant tumor of the skin, have been reported. Hence, lectin- and proteoglycan immunohistochemistry was performed on paraffin wax material of 9 cases of Merkel cell carcinomas characterized by cytokeratin and neurofilament immunohistochemistry. The lectin binding pattern of tumor cells varied between lectins with different sugar binding specificities, while within a given nominal sugar specificity intensities were remarkably similar between tumors from different patients. The most intensive reaction was observed using Con A (mannose/glucose-specific) followed by LCA with the same specificity and the N-Acetyl glucosamine-specific lectins (WGA, UDA, CMA), while no fucose binding sites were detected (UEA-I). In addition, N-Acetyl galactosamine residues were only occasionally detected. The lectin binding pattern of Merkel cell carcinoma cells indicated that predominantly N-linked glycans and not O-linked glycans, typical for mucins of most epithelia, were present. Hence these tumor cells were relatively undifferentiated and resembled stem cells more closely than differentiated epithelia. The tumor stroma was especially evaluated in this study and showed a lectin reaction, which was intermediate between the tumor cells and extra-tumoral stroma. For example, the reactions of N-Acetyl galactosamine-specific lectins were intensive in the extra-tumoral stroma but nearly negative in tumor cells, while the lectin reaction of the intra-tumoral stroma was similar to the cellular reaction. These results indicated an influence of tumor cells on the stromal constituents. Antibodies against chondroitin type glycosaminoglycans reacted with the tumor stroma and the pericellular substance around the tumor cells most intensely in – and around the major tumor septae which, in general, were well vascularized. The most intensive immunoreactivity was detected using the chondroitin-6-sulfate antibody. The cellular and membrane-associated reaction for heparan sulfate was less intensive in comparison to epidermal cells. In conclusion the pattern of lectin-binding sites, the high chondroitin(sulfate) specific reactivity and the relatively low intensity of heparan sulfate immunohistochemistry indicate a low degree of differentiation and high malignity of the tumors, which is consistent with the clinical behavior of Merkel cell carcinomas.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 48 (1992), S. 742-744 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Plant cell reports 2 (1983), S. 277-280 
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rice (Oryza sativa, L.) lectin is specifically synthesized during seed formation. It accumulates very rapidly between 8 and 16 days post anthesis and reaches its final content 20 days post anthesis. The rate of synthesis of this protein dramatically increases during the developmental phase coinciding with the rapid lectin accumulation. When the lectin accumulation stops, its rate of synthesis declines rapidly and eventually stops in fully mature embryos. It appears, therefore, that rice lectin is a maturation-specific protein.
    Type of Medium: Electronic Resource
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