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  • 1
    Electronic Resource
    Electronic Resource
    Method for Lyophilizing Brain Proteolipid Preparation That Increases Subsequent Solubilization by Detergent (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A frozen mixture of solubilized brain proteolipid proteins in chloroform-methanol is not sublimable in a vacuum. However, when 7 to 10 volumes of benzene were added to a chloroform-methanol solution containing 5 mg of proteolipid protein per ml, the proteolipid proteins remained in solution for a while and the frozen mixture was easily sublimated at 2 mm Hg. Before the addition of benzene, higher concentrations of protein required the acidification of the medium to avoid precipitation of proteolipid proteins. In contrast to what happens when proteolipid proteins are obtained by the evaporation of the organic mixture at room temperature, the protein obtained by lyophilization was soluble in aqueous solutions of ionic and nonionic detergents. Sodium dodecyl sulfate at 0.6 to 0.7% concentration completely solubilized the proteolipid protein obtained by lyophilization. With the nonionic detergents Lubrol WX and Triton X-100, a solubilization between 50 and 65% was achieved. Sodium deoxycholate was practically ineffective. Triton X-100 showed selectivity in solubilizing certain proteins. The role of lipids in the solubilization of proteolipid proteins with detergents is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08010.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The Delipidation of Brain Proteolipid Protein by Ultrafiltration (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: It has been very difficult to prepare the apo-protein moiety of brain white matter proteolipid so that it is completely devoid of complex lipids, without suffering aggregation and protein denaturation. The reason is that complex lipids are tightly bound to the proteolipid apo-protein. Using a new ultrafiltration method, we obtained, in a gradual way and in a relatively short time, more than 99% delipidation in water-saturated n-butanol, with and without 0.1 M acetic acid and recovered up to 86% of the protein with no detectable reducing sugars remaining. The delipidated protein remained in solution and in a relatively nondenatured state for several days. In 1% sodium dodecyl sulfate (SDS)-aqueous media, 90% of the lipids were removed and the yield of recovered protein in solution was near 90%; nearly 6% of the reducing sugars remained in the apoprotein. A higher delipidation was obtained by washing with 0.1 M NaOH. The content of reducing sugars was greater but the protein was less stable. When 10% SDS was employed to dissociate lipid-protein interaction, an almost complete delipidation was obtained and reducing sugars disappeared.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb11323.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Ontogenesis of Muscarinic Receptors and Acetylcholinesterase Activity in Various Areas of Chick Brain (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 37 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Muscarinic receptors, labeled with [3H]quinuclidinyl benzylate (3H]QNB), and acetylcholinesterase activity were studied in five areas of the developing chick brain: (1) hyperstriatum and neostriatum, (2) paleostriatum, (3) optic lobes, (4) mesodiencephalon and (5) cerebellum. The protein content of these areas, expressed as mg/g tissue and total protein, was determined between day -10 and adulthood. Differences in both determinations were observed among the areas. The binding of [3H]QNB was expressed as density (fmol/mg protein) and total number of receptors (fmol/total protein) in the area. Considerable variations were observed among the areas. The cerebellum showed the lowest receptor density and a large decrease in density and total number of receptors in the adult, which may reflect a change in neuronal population. Acetylcholinesterase, in certain areas, accompanied the changes in receptor concentration, but the timing and rate of increase had special features in each case. The most striking one was the cerebellum, in which the enzyme increased steadily postnatally, while the muscarinic receptors dropped to very low values.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb06321.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and Chemical Characterization of a W2 Protein from Brain Myelin (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Starting from a pellet of beef brain myelin insoluble in chloroform/ methanol (2:1, vol/vol) (Wolfgram protein fraction), a pure W2 protein with apparent molecular weight of 52,000 was isolated by a simple preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis method. A comparative chemical analysis was carried out between purified W2 and a standard tubulin. Glutamic acid and arginine were the N-terminals detected. Similar peptide maps and amino acid composition were also found in both proteins. Immunological cross-reactivity was detected when W2 protein was tested against antitubulin serum. These results suggest that W2 protein could have a tubulin-like protein nature that is associated with the myelin membrane and could play a role in the myelination process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb03973.x
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    Paper (German National Licenses)
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