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  • 1
    Electronic Resource
    Electronic Resource
    FRACTIONATION OF BRAIN MACROMOLECULES–I. (1962)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 9 (1962), 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.1471-4159.1962.tb09473.x
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of the Mannose-Rich Oligosaccharide Chains of Concanavalin A-Binding Glycopeptides Derived from Beef Brain Glycoproteins (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 41 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A neutral, mannose-rich, concanavalin A (Con A)-binding glycopeptide fraction was obtained by proteolytic digestion of defatted beef brain tissue. Hydrazinolysis followed by gel filtration of the reaction products provided three oligosaccharides. A portion of each oligosaccharide was treated by exhaustive digestion with α-mannosidase. Another portion was subjected to selective acetolysis of Manαl-6Man linkages, providing two fragments that were recovered by gel filtration. The structure of the intact oligosaccharides, as well as the fragments obtained by selective acetolysis and enzymatic treatment, were resolved by gas-liquid chromatographic-mass spectrometric analysis. The structures of the three oligosaccharides were: (a) Manαl-2Manαl-6(Manαl -3)Manαl-6(Manαl-2Manαl-2Manαl 3)Manβ1-4-N-acetylglucosamine (GlcNAc)β -4N- acetylglucosaminitol (GlcOLNAc); (b) Manαl -2Manαl -6(Manαl -3)Manαl-6(Manαl-2Manαl-3)-Manβ1-4GlcNAcβl -4GlcOLNAc; and (c) Manαl -6(Manαl-3) Manαl - 6(Manαl - 3)Manβl -4GlcNAc-βl - 4GlcOLNAc. These structures account for 15–20% of the glycoprotein-carbohydrate of whole beef brain and most of the oligosaccharides that demonstrate a high affinity for Con A. In view of the large number of Con A-binding glycoproteins in brain tissue, it appears that many of these different glycoproteins must contain structurally identical oligosaccharides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb04746.x
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  • 3
    Electronic Resource
    Electronic Resource
    FRACTIONATTON OF BRAIN MACROMOLECULES—II. ISOLATION OF PROTEIN-LINKED SIALOMUCOPOLY-SACCHARIDES FROM SUBCELLULAR, PARTICULATE FRACTIONS FROM RAT BRAIN (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 11 (1964), 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.1471-4159.1964.tb11604.x
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  • 4
    Electronic Resource
    Electronic Resource
    Localization of Hyaluronectin in Oligodendroglial Cells (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Astroglia and oligodendroglia in primary cell cultures were identified by immunohistochemical staining with antiglial fibrillary acidic protein and anticerebroside antisera, respectively. The antiserum to hyaluronectin (HN) was utilized to show that this hyaluronic acid-binding glycoprotein was localized in the Oligodendroglial cell. This is consistent with the recent finding that HN is localized in the node of Ranvier. Astroglia did not react with antihyaluronectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb11324.x
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  • 5
    Electronic Resource
    Electronic Resource
    ISOLATION AND DETERMINATION OF NON-DIFFUSIBLE SIALOFUCOHEXOSAMINOGLYCANS DERIVED FROM BRAIN GLYCOPROTEINS AND THEIR ANATOMICAL DISTRIBUTION IN BOVINE BRAIN (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Glycoproteins in brain tissue were assayed by determining the amount of N-acetylneuraminic acid (NANA), hexosamine, hexose, and fucose present in glycopeptides released by the proteolytic action of papain on the defatted protein residue that remains after treatment of the sample with chloroform-methanol (2:1 and 1:2, v/v). Diffusible and non-diffusible glycopeptides (sialofucohexosaminoglycans) were released by proteolysis. The procedure demonstrated that successive treatment of brain tissue with chloroform-methanol (2:1, v/v) and chloroform-methanol (1:2, v/v) removed all of the gangliosides present in the tissue.A 1 hr autolysis of rat brain tissue had no effect on the amount of glycopeptides recovered from the tissue. The carbohydrate composition of the non-diffusible sialofucohexosaminoglycans was also unaffected.Areas of the brain that are enriched in neuronal cell bodies contained a higher concentration of gangliosides and glycoproteins than areas that consist largely of myelinated fibre tracts. On the other hand, there was a greater concentration of glycoprotein relative to that of gangliosides in areas that consist predominately of myelinated fibre tracts and glia than in areas enriched in neuronal cell bodies. The concentration of non-diffusible sialofucohexosaminoglycans in whole bovine brain was less than that in whole rat brain. The non-diffusible sialofucohexosaminoglycans from whole bovine brain contained less fucose and NANA per mole of hexosamine and hexose than non-diffusible sialofucohexosaminoglycans isolated from whole rat brain. The non-diffusible sialofucohexosaminoglycans isolated from bovine cerebral white matter were lower in fucose and NANA content per mole of hexose and hexosamine than those isolated from other brain areas. It is suggested that the fucose and NANA content of the non-diffusible sialofucohexosaminoglycans associated with myelinated axons and (or) glia is less than that of the non-diffusible sialofucohexosaminoglycans associated with the nerve cell body.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1969.tb05950.x
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  • 6
    Electronic Resource
    Electronic Resource
    THE INTRACELLULAR DISTRIBUTION OF GLYCOLYTIC AND TRICARBOXYLIC ACID CYCLE ENZYMES IN RAT BRAIN MITOCHONDRIAL PREPARATIONS (1963)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 10 (1963), 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.1471-4159.1963.tb13671.x
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of Hyaluronectin by C-6 Glial Cells at High Density (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: Hyaluronectin, a brain glycoprotein that has been localized to the nodes of Ranvier in vivo and to oligodendrocytes in primary cultures of neonatal rat brain cells, was shown by using an unlabeled immunoperoxidase method to be present in C-6 glial cells grown to high density. The density-dependent expression of this glycoprotein is in accordance with the known properties of the glial stem cells, i.e., induction of differentiated properties such as 2′,3′-cyclic nucleotide-3′-phosphohydrolase, glutamine synthetase, S-100 protein, and glial fibrillary acidic protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07174.x
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  • 8
    Electronic Resource
    Electronic Resource
    Specific alterations in phosphorylation of cytosol proteins from differentiating neuroblastoma cells grown in culture (1977)
    [s.l.] : Nature Publishing Group
    Nature 265 (1977), S. 238-240 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Cells of the previously defined3 clone NBP2 were cultured and maintained as previously described1. Differentiation was induced by treating the cells for 3 days with 4-(3-butoxy-4-methoxybenzyl)-2-imidazolidinone (R020-1724)11, a rather specific inhibitor of cyclic AMP phosphodiesterase14,15. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/265238a0
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  • 9
    Electronic Resource
    Electronic Resource
    Synthesis of sulfated glycoproteins by glial precursor cells (1986)
    Springer
    Neurochemical research 11 (1986), S. 1193-1201 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Populations of enriched glial precursor cells and astrocytes isolated from primary cultures of newborn rat brain were used to study the synthesis of sulfated glycoproteins. Both cell types incorporated [3H]glucosamine and [35S]sulfate into carbohydrate side chains of proteoglycans and glycoproteins. The rate of incorporation of [3H]glucosamine into the oligosaccharides and the pattern of distribution of the label into high mannose and complex glycopeptides recovered from the glycoproteins appeared to be similar for the two glial cell types. However, clear differences were noted in the rate of oligosaccharide sulfation activities. Thus the cultures of precursor glia were about four times more active than cultures enriched in astroglia in their ability to incorporate [35S]sulfate into glycoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965947
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  • 10
    Electronic Resource
    Electronic Resource
    Changes in glycoprotein carbohydrate content in the aging human brain (1986)
    Springer
    Neurochemical research 11 (1986), S. 579-588 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract There is no significant change in the concentration, per gram of fresh tissue, of the total carbohydrate associated with brain glycoproteins as the human brain ages from 25 to 85 years. Nevertheless, notable shifts in the concentration of varied types of oligosaccharides do occur. The concentration and percentage of total glycopeptide-carbohydrate recovered from the whole brain represented by the N-glycosidically linked complex siablooligosaccharides of the tri-and tetraantennary type show a marked decline with age. On the other hand, the N-linked mannose high oligosaccharides of the ovalbumin type, the N-linked biantennary sialoglycopeptides of the transferrin type, and the O-linked oligosaccharides show an increase as the brain ages. Other age related changes that were noted include an increase in the number of sulfate ester groups associated with the N-linked sialoglycopeptides and a decrease in the number of phosphorylated high mannose oligosaccharides as the brain ages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965327
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