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  • 1
    Electronic Resource
    Electronic Resource
    Cardiotoxic protein from edible mushrooms (1974)
    [s.l.] : Nature Publishing Group
    Nature 252 (1974), S. 235-237 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Flammulina velutipes fruits throughout the year. Its cap, initially ovoid and yellow becomes, within one or two days, flat and yellowish brown with an edge of lighter colour. The cap reaches a diameter of 2 cm; the stem achieves a length of 15cm and a diameter of 0.5cm. This mushroom has little ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/252235a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of phospholipase A2 activation by plasmin in cultured bovine endothelial cells (1996)
    Springer
    Journal of biomedical science 3 (1996), S. 59-66 
    Details
    ISSN: 1423-0127
    Keywords: Plasmin ; Calcium influx ; Cytosolic phospholipase A2 ; Endothelial cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Treatment of cultured bovine carotid artery endothelial cells with 0.1 µM human plasmin has been reported to induce a receptor-mediated short burst of arachidonate release, which is a pertussis toxin-sensitive and extracellular calcium-dependent reaction. Plasmin-induced calcium influx in cells was significantly inhibited by pretreatment with pertussis toxin, indicating that the former was coupled with a pertussis toxin-sensitive guanosine 5′-triphosphate (GTP)-binding protein. Plasmin significantly induced the formation of lysophosphatidylcholine but not lysophosphatidylethanolamine. A cellular phospholipase A2 with an arachidonyl specificity at the sn-2 position of phosphatidylcholine, which required submicromolar calcium, was identified as a cytosolic phospholipase A2 by immunoblot analysis. By a cell-free enzyme activity assay and immunoblot analysis, plasmin was found to induce a translocation of the cytosolic phospholipase A2 from the cytosol to the membrane. Taken together, the results suggest that plasmin bound to its putative receptor and activated a GTP-binding protein coupled to calcium influx channel, followed by translocation and activation of cytosolic phospholipase A2 in endothelial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02253580
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  • 3
    Electronic Resource
    Electronic Resource
    The various effects of fractionated oxidized low density lipoproteins on the growth of smooth muscle cells in culture (1999)
    Springer
    Journal of biomedical science 6 (1999), S. 260-268 
    Details
    ISSN: 1423-0127
    Keywords: Oxidized low density liporpotein ; Lysophosphatidylcholine ; Smooth muscle cells ; Protein kinase C
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The effects of fractionated oxidized low density lipoproteins (oxidized LDL) on the growth of vascular smooth muscle cells (VSMC) and their relationship to the formation of lysophosphatidylcholine (lyso-PC) as well as the activation of protein kinase C (PKC) were studied. VSMC were isolated from porcine aorta by explant culture. LDL was isolated from porcine blood by sequential ultracentrifugation and oxidized LDL was obtained by incubating LDL with 5 µM CuSO4 at 37° C for various lengths of time. Our results showed that LDL oxidized for 12 h and eluted from fast protein liquid chromatography at 43 min inhibited the growth of VSMC, and that LDL oxidized for longer than 48 h and eluted at 48 min stimulated the growth of VSMC. The formation of lyso-PC in the oxidized LDL correlated well with its stimulatory effect, suggesting that lyso-PC is responsible for the mitogenic effect of oxidized LDL. This stimulatory effect of oxidized LDL was inhibited by staurosporine, a PKC inhibitor. Treatment with oxidized LDL increased the activity of membrane PKC, but it decreased that of cytosolic PKC, suggesting the translocation of PKC from cytosol to the membrane in the presence of oxidized LDL. These results suggested that the oxidized LDL-stimulated VSMC growth was mediated by the formation of lyso-PC and the activation of PKC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02253567
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of proteins by reductive alkylation with hydrophobic aldehydes (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 23 (1981), S. 855-861 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new method is described for the immobilization of enzymes and other proteins onto hydrophobic gels. Trypsin, for example, can be quantitatively immobilized by reaction with sodium cyanoborohydride and dodecyladehyde-coated Octyl-Sepharose. Noncovalent interactions between the hydrophobic gel and approximately 10 resulting dodecylamino groups in the modified enzyme bind it very strongly but do not affect its ability to hydrolyze benzolarginine ethyl ester. The same procedure can also be used to immobilize E. Coli asparaginase and yeast alcohol dehydrogenase in high yield.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260230415
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