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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Gangliosides were isolated from purified human myelin in a yield of 62 μg of lipid-bound sialic acid per 100 mg of dry myelin. Sialosylgalactosyl ceramide (G7) was found to be a major component of the ganglioside fraction, amounting to 15 per cent of the total sialic acid. It accounted for 10 per cent of lipid-bound sialic acid in adult human white matter, making it the third most abundant ganglioside on a molar basis. These results were obtained with an improved method for isolating total gangliosides in high yield, by employing DEAE-Sephadex column chromatography. Myelin from other mammalian species had considerably less G7, and there were also indications of maturational changes. Both 2-hydroxy and unsubstituted fatty acids were components of the ceramide unit, in a ratio of 3:2, respectively. The overall fatty acid pattern was very similar to that for myelin cerebroside and sulphatide. Long-chain bases included only C18 species, with sphingosine predominating (〉90 per cent). These observations suggest a metabolic relationship between G7 and either cerebroside or sulphatide.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The two-site immunoradiometric assay (two-site IRMA) for a specific protein of the nervous system, S-100, is carried out by reaction of the S-100 protein solution with a solid-phase anti(S-100) followed by a second reaction in which the insoluble product is incubated with purified, radioactive anti(S-100). Unreacted labeled antibodies remain in solution and are washed away. As the amount of S-100 increases, the radioactivity in the solid-phase increases. The most significant assay variable is the effect of calcium on the assay dose-response. 0.1 mM-EDTA causes a total inhibition of the dose-response curve which is reversed by increasing the concentration of calcium ions. The dose-response reaches a maximum at 1.0mM-Ca2+. then becomes progressively inhibited as the Ca2+ concentration is increased further. Previous immunochemical studies of S-100 which did not allow for this effect must now be interpreted with caution.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 14 (1967), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The brain-specific antigens 14·3·2, GFA, A5, F3, D1, D2, D3 and C1 were quantitated in a short-term astroglial cell culture taken as a model of glial cells, and in synaptosomes, synaptosomal membranes and synaptic vesicles as neuronal material. Furthermore, the antigens were quantitated in newborn rat brain, as this served as the starting material for the cell culture. The membrane antigens C1, D1, D2 and D3 were absent from the cultured astroglia, indicating a neuronal origin for these antigens. C1 was enriched 3-fold in synaptosomes and synaptosomal membranes and more than 10-fold in synaptic vesicles indicating that this antigen might be a marker protein for nerve endings. The name Synaptin is introduced for this antigen. Conversely, the data on the antigens D1, D2 and D3 indicated that these antigens were not restricted to the synaptosomes although they were of neuronal origin. Trace amounts of the cathodal part of the heterogeneous cytoplasmic antigen 14·3·2 were present in the cell culture, possibly originating from a few contaminating neurons. The cytoplasmic antigens A5 and F3 were found both in the astroglial culture and in the synaptosomal fraction. F3, however, was found in low concentration in the synaptosomes and 3-fold enriched in newborn rat brain compared to rat brain from 35-day-old rats or to 21-day-old brain cell cultures. It was therefore regarded as a brain specific fetal antigen. The antigen GFA was highly enriched in the astroglial culture compared to whole brain and only trace amounts were found in the synaptosomal fraction supporting the astroglial origin of this antigen.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Gangliosides were isolated from plaque tissue and normal appearing white matter of multiple sclerosis (MS) brain. All four plaques showed decreased ganglioside concn relative to normal human white matter on a wet wt basis, but significant elevation in terms of dry wt. The wet wt and dry wt concn of MS white matter gangliosides showed smaller but statistically significant decreases below normal. Thin-layer patterns of the plaques showed several departures from normal white matter, including decrease of G4 and G5, and complete loss of G7 (sialosylgalactosylceramide). Most of the plaques had significant elevation of G2A and G3A along with increases of the slower-migrating polysialogangliosides. An additional ganglioside was present between G2 and G2A which was not seen in normal white matter. The TLC pattern of MS white matter gangliosides was essentially normal. The evidence for a general decrease of acidic lipids within normal appearing white matter is discussed.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Wallerian degeneration of the optic nerves of the rat was induced by removal of the eyes. After 54, 66, 76 or 90 days of degeneration a myelin fraction of the nerves was obtained by the procedure of Laatschet al. (1962). The yield of myelin from the degenerated nerves was decreased, but the isolated myelin appeared to be morphologically normal. The proportion of cholesterol in the myelin lipids was slightly increased, whereas that of the ethanolamineglycerophosphatides was decreased and galactolipids were normal. After one‘cycle’of myelin purification, the high-molecular-weight fraction formed a much greater percentage of the total protein in myelin isolated from degenerated optic nerves. After 2–3‘cycles’of purification, the distribution of protein in myelin isolated from degenerated and normal optic nerves was similar, an observation suggesting that the high-molecular-weight fraction in‘1-cycle myelin’from degenerated optic nerves may have been partly attributable to contamination. With the possible exception of ethanolamineglycerophosphatides, our data suggest that there was no preferential breakdown of myelin lipid constituents nor of protein constituents during Wallerian degeneration of rat optic nerve. As assessed by SDS-gel electrophoresis of the water-insoluble particulate fraction, the percentage of myelin protein was markedly decreased after 76 days of degeneration. However, the major myelin protein constituents in this fraction (the two basic proteins and proteolipid protein) appeared to decrease in the same relative proportions.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 10 (1963), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 17 (1970), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Quantitative analyses of white matter from four brains of patients with multiple sclerosis (MS) and four control brains were carried out for total and soluble proteins, individual lipid fractions, and their corresponding fatty acids. In three specimens from two of the MS brains there were reductions of cerebrosides and of the C20:1 acid in the ethanolamine glycerophosphatide (EGP) fraction and a slight increase of tetraenes and trienes, while all other components were present in concentrations similar to those in the controls. In three other samples from two of the MS brains, galactolipids were deficient to a greater extent than cholesterol, EGP or CGP (choline glycerophosphatide), while proteins were within the control range. In samples where thinning of myelin was observed in Luxol-blue stained sections, there were proportional decreases of all components. The percentage of C20:1 acid in the EGP fraction was reduced in two of three myelin preparations from corresponding samples of MS white matter, and that of C24:1 acid in the cerebroside fraction was reduced in all three MS myelin preparations when compared with the two controls. The data suggest that inadequacy of the fatty acid elongation process together with deficits of cerebrosides represent one of the early biochemical lesions in the white matter of the MS brain.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 15 (1982), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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