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  • Articles: DFG German National Licenses  (2)
  • 1980-1984  (2)
  • 1983  (2)
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  • Articles: DFG German National Licenses  (2)
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Years
  • 1980-1984  (2)
Year
  • 1
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Almond glycopeptidase is an enzyme which cleaves specifically β-aspartylglucosylamine linkages in glycoproteins with asialo-carbohydrate moieties. With this enzyme, it was possible to demonstrate the localization of asparagine-linked oligosaccharides in glycoproteins of human placenta and umbilical cord tissues. In these tissues, the oligosaccharides were shown to react positively for a series of histochemical procedures for neutral complex carbohydrates such as periodic acid-Schiff (PAS), peroxidase-labelledRicinus communis agglutinin-I-diaminobenzidine (PO-RCA-DAB) and concanavalin A-peroxidase-diaminobenzidine (Con A-PO-DAB). The asparagine-linked carbohydrates were localized in the placental villi, blood vessels and perivascular tissues and the umbilical cord blood vessels and matrix. The results of previous biochemical analyses performed upon the same tissues (Takahashiet al., 1981) have corroborated the results of the histochemical studies. The present results appear to substantiate the usefulness of almond glycopeptidase for the histochemical demonstration of the particular oligosaccharides of glycoproteins in tissues in general.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Systematic study of polarization of projectile like fragment12B in14N induced reactions on light mass-number targets has been continued. A large positive polarization at small energy loss region was observed for an27Al target at various reaction angles. Polarization is studied as a function of kinetic energy and reaction angle of12B in terms of a classical frictional force.
    Type of Medium: Electronic Resource
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