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  • 1
    ISSN: 1432-1106
    Keywords: Myelin deficiency ; Mutant mice (msd) ; Sulphatide synthesis ; Cerebroside sulphotransferase ; Developmental changes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. The activity of the sulphotransferase involved in the synthesis of sulphatides, 3′-phosphoadenosine-5′-phosphosulphate cerebroside sulphotransferase (PAPS-CST), was determined in the developing CNS of the myelin synthesis deficiency mutant mouse (msd) and compared to that in control animals. There was a decrease of the PAPS-CST activity in msd mouse in the period from 8 to 26 days. The developmental curve of PAPS-CST activity in msd mice brains essentially paralleled that in normal animals, with a maximum at about 19 days. 2. Basic enzyme properties, such as Km, optimum pH, and heat inactivation, were not affected by the mutation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Clinica Chimica Acta 38 (1972), S. 147-153 
    ISSN: 0009-8981
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Physics Letters A 179 (1993), S. 343-347 
    ISSN: 0375-9601
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Physics Letters A 96 (1983), S. 183-187 
    ISSN: 0375-9601
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Snell dwarf mice (dw/dw) and normal mice (+/?) were injected with thyroxine (T4) (1 μg/animal, four injections) and growth hormone (GH) (20 μg/animal, four injections) from the 5th to the 15th day of life. In the untreated dw/dw mouse brain, the specific activities of UDP-galactose:ceramide galactosyltransferase (CGalT), PAPS:cerebroside sulfotransferase (CST), and 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNP) were decreased by 28, 25, and 37%, respectively, compared with the control untreated +/? mice. The major effect of T4 was an increase of the brain CNP in the +/? mice (+40%) and dw/dw mice (+111%). The treatment with T4 also brought to normal the level of CGalT in dw/dw brain; a somewhat less marked effect on CST was observed. The treatment with GH had a great stimulatory effect on CNP: the specific activity of this enzyme increased by 40 and 69% in +/? and dw/dw mouse brain, respectively. On the contrary, no effect of GH on the CGalT activity was observe in this study. Our results suggest that T4 and GH may have both independent and complementary actions on the myelin-associated enzymes during the early postnatal period of brain development.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 47 (1986), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract A new method for purification of UDPgalactose: ceramide galactosyltransferase (EC 2.4.1.45) is described. The principal steps involved solvent extraction at—70°, Triton X-100 extraction, and DEAE-Sephadex and Blue Sepharose chromatography. The active configuration of the enzyme was stabilized by phospholipids and a rapid loss of enzymatic activity was observed after removal of these lipids. The inactive enzyme could be fully reactivated in the presence of brain phospholipids dispersed in a Triton X-100-containing buffer. The purified enzyme preparation showed two major components by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate with apparent molecular weights of 50–70,000. The 53,000-dalton protein was isolated by preparative gel electrophoresis in the presence of sodium dodecyl sulfate and used to produce antibodies against UDPgalactosexeramide galactosyltransferase.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 37 (1981), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: UDP-galactose:ceramide galactosyltransferase (CGalT, EC 2.4.1.45) and UDP-glucose:ceramide glucosyltransferase (CGlcT, EC 2.4.1.80) were determined in the glial cell lines G26-20, G26-24, C6, and C6TK−. The enzymatic assay for CGalT in cultured glial cells was complicated by a rapid conversion of UDP-galactose to UDP-glucose, due to the elevated UDP-galactose-4′-epi-merase activity in certain glial cell clones. It seems that mechanisms regulating UDP-galactose-4′-epimerase activity and levels of UDP sugars in the glial cell lines differ from those in brain tissue. Compared with the maximum activity of CGalT in the myelinating rat brain, the enzyme activities in the oligodendroglioma clonal cell lines G26–20 and G26–24 were 16–30 times lower. On the other hand, CGalT levels in G26-20 and G26-24 cells were comparable to the values found in young rat brain before myelination starts. No CGalT activity could be detected in C6 or C6TK− cells by the method used in this study, whereas CGlcT activity was found in all glial cell lines tested and its levels were close to the values observed in the young rat brain.
    Type of Medium: Electronic Resource
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  • 8
    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: The subcellular and submicrosomal distributions of four glycolipid-synthesizing transferases were studied in young rat brains.(1) Two galactosyl transferases involved in the synthesis of cerebrosides, the cerebroside sulphotransferase which catalyses the synthesis of sulphatides, and the glucosyl transferase which plays an important role in the ganglioside biosynthesis were localized essentially in the microsomal fraction. Only low activities were detected in the crude mitochondrial and synaptosome-enriched fractions.(2) A comparison of the activities of these enzymes in the crude myelin and two myelin subfractions showed that the galactosyl transferases and the cerebroside sulphotransferase had similar activities in the crude myelin and myelin-like fractions. A considerable galactosyl transferase activity was found in purified myelin. In this respect these two enzymes were different from cerebroside sulphotransferase, whose activity was much lower in purified myelin. On the other hand, glucosyl transferase had a relatively low specific activity in all three myelin fractions. Analysis of different markers showed that the activities were considerably higher than those expected from the maximum microsomal contamination calculated.(3) Subfractionation of the microsomes demonstrated that the galactosyl transferases were more concentrated in the lower parts of the gradient, containing vesicles with attached ribosomes. Cerebroside sulphotransferase and glucosyl transferase were found predominantly in the upper and intermediate parts of the gradient, which were composed essentially of smooth-surfaced vesicles and membrane fragments. Chemical analysis of submicrosomal fractions confirmed the morphological observations.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: (1) Brain composition and developmental changes were investigated in a mutant (‘Jimpy’) mouse characterized by a severe myelin deficiency.(2) Significantly lower cholesterol, phospholipid and galactolipid values were observed, and the accumulation of these lipids during the myelination period was markedly reduced or absent.(3) The most remarkable feature of ‘Jimpy’ brain was a very small galactolipid content. In 29-day-old mutants the concentration of galactolipids was 0-18 μ moles/g wet wt., representing a 46-fold decrease when compared to values determined in normal mice.(4) There was no such striking change in the distribution of different phospholipids. However, lowered relative amounts of some phospholipids, e.g. ethanolamine plasmalogen, sphingomyelin and phosphatidylserine, were observed in ‘Jimpy’ brain.(5) Protein content was also lower in mutant brains and showed an absolute decrease after 23 days of life.(6) These data support the statement that the process of myelination is disturbed at an early stage, resulting in a deficiency of mature myelin sheaths and leading probably to the breakdown of primitive myelin structures.
    Type of Medium: Electronic Resource
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  • 10
    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— The phospholipid composition of, and the incorporation of labelled phosphorus into the different phospholipids of rat and calf retina have been studied. The influence of various conditions, such as dark and light adaptation, during the preparation of retina, lipid extraction and incubation of retina with radioactive phosphorus was investigated.The phospholipid composition of rat retina did not differ significantly from that of calf retina and the different conditions of preparation and incubation did not modify the distributions.The specific radioactivities of the different phospholipids of calf and rat retina, incubated in the presence of 32P, distinguished in both species two groups of components characterized by the rate of labelling. Phosphatidic acid (PA) and inositol glycerophospholipids (PI) belonged to the first group and showed the highest uptake of labelled phosphorus; the second group, comprising choline glycerophospholipids (PC), serine glycerophospholipids (PS), sphingomyelin (SP), ethanolamine glycerophospholipids (PE) and cardiolipin (CL) showed low incorporation activities. Only SP was labelled differently in rat and calf retina. With the exception of PS, there was no evidence for the influence of light on the turnover of individual phospholipids. The finding that PS showed higher specific radioactivities when adaptation and incubation proceeded in the dark, seems to be of interest and needs further study.
    Type of Medium: Electronic Resource
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