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  • Articles: DFG German National Licenses  (7)
  • 1985-1989  (2)
  • 1975-1979  (5)
Source
  • Articles: DFG German National Licenses  (7)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Split chromatographic spot produced by supposedly single gangliosides treated with trichloroacetic acid—phosphotungstic acid reagent (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04467.x
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    GLYCOPROTEINS AND GLYCOLIPIDS OF SUBCELLULAR FRACTIONS FROM BOVINE RETINA. INCORPORATION OF MANNOSE AND SIALIC ACID (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Endogenous lipids and proteins of bovine retina subcellular fractions were labelled from CMP-[3H]NeuNAc and GDP-[14C]mannose. The bulk of NeuNAc and mannose transfer activity was in membranes other than those from the rod outer segment (ROS). Lighter and heavier membranes, obtained from ROS free membranes by density gradient centrifugation, were the most active for the incorporation of NeuNAc and mannose, respectively. NeuNAc bound to a lipid indistinguishable from gangliosides, and a lipid that contains mannose (mannolipid-I) were found in the fraction extractable with chloroform-methanol (2:1, v/v). Mannose was also incorporated into a lipid fraction extractable with chloroform-methanol-water (1:1:0.3, by vol) (mannolipid-II). Mannolipid-I and mannolipid-II were labile to mild acid hydrolysis. In the presence of ROS free membranes, radioactivity of mannoli-pid-I was transferred to mannolipid-II and from this to proteins. Analyzed by sodium dodecyl sulphate polyacrylamide gel electrophoresis, the proteins labelled from GDP-mannose migrated as a broad peak covering the range of molecular weights 20,000–30,000 and including the zone of rhodopsin migration. The proteins labelled from CMP-NeuNAc showed four radioactive peaks that were coincident with three out of four periodic acid-Schiff (PAS) positive bands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10631.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    THE SITE OF SYNTHESIS OF GANGLIOSIDES IN THE CHICK OPTIC SYSTEM (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 33 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract– In the retinas of 1-day-old chickens that received an intraocular injection of N-[3H]acetylmannosamine the labelling of N-acetylneuraminic acid and CMP-N-acetylneuraminic acid increased for at least 8 h and that of gangliosides for at least 24 h after injection. In the optic tectum contralateral to the injected eye at 8 h after the intraocular injection, the labelling of gangliosides exceeded the labelling of gangliosides in the ipsilateral tectum by approx 20-fold. In the contralateral tectum the highest concentration of labelled gangliosides was in subfractions enriched in synaptosomes and synaptic plasma membranes. No significant contralateral ipsilateral differences were found in the acid soluble substances of the tectum. In the optic tectum, labelled gangliosides appeared earlier in the neuronal perikarya than in synaptosomes when the injection was intracranial. Conversely, when the injection was intraocular the labelling appeared earlier in the synaptosomes than in the neuronal perikarya. The radioactivity pattern of the optic tectum gangliosides resembled the pattern of retina gangliosides when N-[3H]acetylmannosamine was injected intraocularly, but when N-[3H]acetylmannosamine was given intracerebrally the radioactivity pattern resembled that of optic tectum gangliosides. Intraocular injection of colchicine or vinblastine did not affect the labelling of retinal gangliosides from N-[3H]acetylmannosamine injected into the same eye but prevented the appearance of labelled gangliosides in the optic tectum. In vitro the ganglioside glycosylating activity of optic tectum synaptosomes and synaptic plasma membranes was between 6 and 10-fold lower than that found in the optic tectum neuronal perikarya. These findings support the notion that the main subcellular site of synthesis of neuronal gangliosides is in the neuronal perikarya, from which they are translocated to the nerve endings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb09912.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Posttranslational Incorporation of [14C]Arginine into Rat Brain Proteins. Acceptor Changes During Development (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 44 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Many of the cytosolic proteins of the rat brain appear to have the capacity to incorporate l-[14C]arginine posttranslationally. Scanning of the electrophoretic pattern of the labeled proteins showed two main radioactive peaks: peak A, found in the region of proteins of MW above 200 kD, and peak B, found in the region of 33 kD. The ratio of peaks A/B tends to decrease with the age of the rats. Another zone of radioactivity has an apparent MW similar to that of albumin (approximately 66 kD). No differences were found between the effects of ionic strength and of inhibitors on the arginyl transferase of brain and those described for the transferases of other organs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb12865.x
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Light inhibits the labelling of gangliosides in chicken retina (1975)
    [s.l.] : Nature Publishing Group
    Nature 257 (1975), S. 492-493 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Labelling of retinal gangliosides in chickens maintained in the dark was greater than in those exposed to light (Table 1, experiments 1 and 2). Results were similar when one eye was occluded (experiment 4). In the latter case the difference was smaller and so the possibility remained that in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/257492a0
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Trisialoganglioside synthesis by a chicken brain sialyltransferase. Comparative study with the similar reaction for the synthesis of disialoganglioside (1977)
    Springer
    Molecular and cellular biochemistry 16 (1977), S. 63-70 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary An enzyme preparation from embryonic chicken brain catalyzes the transfer of sialic acid from CMP-N-acetylneuraminic acid to ceramide-Glc-Gal(NeuAc-NeuAc)-GalNAc-Gal (GDlb) to form ceramide-Glc-Gal(NeuAc-NeuAc)-GalNAc-Gal-NeuAc (GTlb). The sialyltransferase activity was measured during the development of the embryo, the subcellular distribution of this activity was determined and several kinetic properties of the reaction were ex-amined. A comparative study with the similar reaction involved in the transfer of sialic acid to the terminal galactose in ceramide-Glc-Gal(NeuAc)-GalNAc-Gal (GMl) was made. The results obtained in this comparative study suggest that the transfer of sialic acid in both reactions is catalyzed by the same enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01732045
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Optic nerve integrity is required for light to affect retina ganglion cell gangliosides (1986)
    Springer
    Neurochemical research 11 (1986), S. 1083-1089 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The labeling of retina ganglion cell and optic tectum gangliosides after an intraocular injection ofN-[3H]acetylmannosamine ([3H]ManNAc) is higher in chickens exposed to light than in those maintained in darkness (1,2). In the present work we studied whether the signal for the higher labeling of ganglion cells in light originates in the photoreceptor layer or comes from the nerve terminal. For this purpose the labeling of ganglion cell gangliosides was determined in light and dark in chickens with one optic nerve severed. The results showed that the effect of light occurred only in the eye normally connected to the optic tectum. In the eye with its optic nerve severed, no difference was observed between the labeling of gangliosides in animals in light and dark, having both groups the labeling values of the normal eyes exposed to light. The results indicate that the information that decreases labeling in darkness or accelerates it in light originates in the nerve terminal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965596
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    Paper (German National Licenses)
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