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  • Articles  (3)
  • hemagglutinin  (3)
  • 1995-1999  (3)
  • 1975-1979
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 52 (1996), S. 540-543 
    ISSN: 1420-9071
    Keywords: Lectin ; hemagglutinin ; platelet ; aggregation ; inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Lectins from four marine algal species were examined for interaction with human platelets. The lectin designated hypnin A, from the red algaHypnea japonica, inhibited adenosine diphosphate (ADP)-or collagen-induced human platelet aggregation in a dose-dependent manner. Complete inhibition was observed at concentrations of 100 and 5 μg/ml of the lectin with, ADP (2 μM) and collagen (0.2 μg/ml)-induced platelet aggregation, respectively. At the inhibitory concentration of 0.5 to 100 μg/ml, the lectin did not induce aggregation of resting platelets. Lectins from the other three algal species also inhibited ADP-induced human platelet aggregation. These results indicate that the algal lectins are a new group of inhibitors and may be useful to study glycoconjugates on platelet membranes and to design novel platelet aggregation inhibitors.
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  • 2
    ISSN: 1573-5176
    Keywords: Eucheuma serra ; hemagglutinin ; lectin ; isolectin ; mitogenic activity ; carbohydrate-binding specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aqueous ethanolic extracts from five species of the genus Eucheuma (Rhodophyta) i.e. E. serra, E. amakusaensis, E. cottonii, E. gelatinae and E. denticulatum, were examined for hemagglutinating activity with vertebrate erythrocytes. All the extracts tested agglutinated trypsin-treated sheep and rabbit erythrocytes as well as untreated sheep erythrocytes. From the extract of E. serra, which exhibited the highest activity, a lectin was purified by precipitation with cold ethanol followed by gel filtration to exhibit a single band on SDS-PAGE. The yield was surprisingly as high as 1000 mg from 100 g powdered alga. The purified lectin was further separated into two isoforms, designated ESA-1(90 mg) and ESA-2 (890 mg), by ion exchange chromatography. Both lectins showed a single protein band with the same molecular weight of 29 000 on SDS-PAGE and differed from each other only in isoelectric point (pI 4.75 for ESA-1 and pI 4.95 for ESA-2). Biochemical studies revealed that both are monomeric proteins without a carbohydrate moiety. The hemagglutinating activities were stable over a wide pH range and at a relatively high temperature. The activities were inhibited by a number of glycoproteins, but not by any of the monosaccharides and disaccharides tested. The lectins showed strong mitogenic activities for mouse lymphocytes.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of applied phycology 11 (1999), S. 149-156 
    ISSN: 1573-5176
    Keywords: Eucheuma amakusaensis ; Eucheuma cottonii ; Kappaphycus alvarezii ; hemagglutinin ; lectin ; isolectins ; carbohydrate-binding specificity ; mitogenic activity ; N-terminalamino acid sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We previously reported that the red alga Eucheuma serra contains large amounts of mitogenic isolectins (ESA-1 and ESA-2), the hemagglutinating activities of which were strongly inhibited by glycoproteins bearing high mannose-type N-glycans. We therefore further examined two other species, E. amakusaensis and E. cottonii. Several lectins were isolated easily by a combination of extraction with aqueous ethanol, precipitation with cold ethanol, gel filtration, and ion exchange chromatography from both species, respectively. The purified lectins were designated as EAA-1, EAA-2, EAA-3, ECA-1 and ECA-2 after the specific names of both algae. The yields of EAAs and ECAs were as high as 2.8 and 2.7 mg g−1 of dry tissue, respectively, indicating that both species would also be good sources for high lectin yields. The five purified lectins shared the same properties in hemagglutinating activity, mitogenic activity, and hemagglutination-inhibition test in which glycoproteins bearing high mannose-type N-glycans were the most inhibitory. They also had almost identical molecular weight and 20 N-terminal amino acid sequence to each other and to those of ESAs, and only differed in the isoelectric point, indicating that they are isolectins to each other. The study thus demonstrated that several species of Eucheuma contain high yields of lectins homologous between species, suggesting that the genus as a whole may be considered as a valuable source of lectin proteins.
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