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Histochemical demonstration of asparagine-linked oligosaccharides in glycoproteins of human placenta and umbilical cord tissues by means of almond glycopeptidase digestion

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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.

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Authors and Affiliations

  1. Department of Anatomy, Nagoya City University Medical School, Nagoya, Japan

    K. Yamada

  2. Laboratory of Ultrastructure Research, Aichi Cancer Center Research Institute, Nagoya City University Medical School, Nagoya, Japan

    S. Shimizu

  3. Department of Biochemistry, Nagoya City University Medical School, Nagoya, Japan

    N. Takahashi

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  1. K. Yamada
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  2. S. Shimizu
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  3. N. Takahashi
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Yamada, K., Shimizu, S. & Takahashi, N. Histochemical demonstration of asparagine-linked oligosaccharides in glycoproteins of human placenta and umbilical cord tissues by means of almond glycopeptidase digestion. Histochem J 15, 1239–1250 (1983). https://doi.org/10.1007/BF01002742

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  • DOI: https://doi.org/10.1007/BF01002742

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