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  • 1970-1974  (3)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The S-100 protein fraction of pig and sheep brain was purified in 40 per cent yield by a modification of the procedure of Moore (1965), which avoided selective loss of S-100 components. The S-100 fraction of both pig and sheep is a mixture of proteins as indicated by acrylamide gel electrophoresis and N-terminal amino acid analysis. Differences in amino acid composition, electrophoretic heterogenity and N-terminal analysis were found.One fraction (fraction A) was isolated by DEAE-Sephadex chromatography from pig brain S-100 protein fraction. It was considered to be a single protein since it migrated as a single band on acrylamide gel electrophoresis and showed a single symmetrical peak during ultracentrifugal analysis. Only one N-terminal amino acid was detected in fraction A. The amino acid composition of this fraction showed minor but significant differences from that of the complete S-100 protein fraction from pig brain. The S-100 protein fraction of both species, as well as fraction A, had similar s20, w values and similar molecular weights (about 20,000) as indicated by gel filtration. These results, together with the immunological data obtained by other authors, suggest that the proteins of the S-100 fraction are closely related; the heterogeneity of the S-100 protein fraction may be of the same type as the lactate dehydrogenase isoenzymes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The Enzyme 2′, 3′-cyclic AMP 3′-phosphohydrolase (CNP) is regarded as a marker for myelin (KURI- HARA and MANDEL, 1970) on the basis of its regional and subcellular distribution (Kurihara and Tsukada, 1967), its ontogenetic characteristics (KURIHARA and TSUKADA, 1968), and its behaviour in two strains of myelin-deficient mutant mice (Kurihara, Nussbaum and Mandel, 1969). However we have isolated highly-purified preparations of neuronal plasma membrane from rat brain synaptosomes which contain this enzyme activity (Morgan, Wolfe, Mandel and Gombos, 1971). Two explanations of this finding are possible. The activity could be due to the presence of myelin, but this explanation is ruled out by electron microscopy and by the low level of cerebrosides in the synaptosomal plasma membrane preparations. Myelin is extremely rich in cerebrosides (norton and Autilio, 1966). The second possibility is that the enzyme, 2′, 3′-cyclic AMP 3′-phosphohyrolase, may also be found in the glial cells from which myelin is derived (Bunge, Bunge and Pappas, 1962). To test our hypothesis that 2′, 3′-cyclic AMP 3′-phosphohydrolase is not a specific marker for myelin, but is also found, in glial cells, we have examined a tumoral glial cell line maintained in myelin-free tissue culture.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 240 (1972), S. 59-59 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR,-It is easy to sympathize with the editor of Nature (239, 182; 1972) because it is obviously very difficult to define precisely the limits of discussion in a general scientific journal. Certainly the criterion that "scientists are more affected than other groups of people" seems reasonably ...
    Type of Medium: Electronic Resource
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