Literature DB >> 7284436

Either high-mannose-type or hybrid-type oligosaccharide is linked to the same asparagine residue in ovalbumin.

H Ishihara, N Takahashi, J Ito, E Takeuchi, S Tejima.   

Abstract

After pepsin digestion, all of the carbohydrates in ovalbumin were recovered in two glycopeptides, Glu-Glu-Lys-Tyr-Asn(CHO)-Leu-Thr-Ser-Val and Glu-Gln-Lys-Tyr-Asn(CHO)-Leu-Thr-Ser-Val. Almond glycopeptidase released quantitatively oligosaccharides from the glycopeptides. The products from both glycopeptides contained both the high-mannose-type oligosaccharides and the hybrid-type oligosaccharides in the same ratio. Thus, either the high-mannose-type or the hybrid-type oligosaccharide is attached to the unique asparagine residue in the ovalbumin molecule.

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Year:  1981        PMID： 7284436     DOI： 10.1016/0005-2795(81)90243-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  The core molecule from type H proteoglycan. Release of mannose-containing oligosaccharides by digestion with N-oligosaccharide glycopeptidase.

Authors:  N Takahashi; H Ishihara; S Tejima; Y Oike; K Kimata; T Shinomura; S Suzuki
Journal:  Biochem J       Date:  1985-08-01       Impact factor: 3.857

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

Authors:  K Yamada; S Shimizu; N Takahashi
Journal:  Histochem J       Date:  1983-12

Review 3.  Current ideas on the significance of protein glycosylation.

Authors:  C M West
Journal:  Mol Cell Biochem       Date:  1986 Nov-Dec       Impact factor: 3.396
  3 in total

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