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Seiichi Takasaki

Researcher at University of Tokyo

Publications -  38
Citations -  1687

Seiichi Takasaki is an academic researcher from University of Tokyo. The author has contributed to research in topics: Glycoprotein & Oligosaccharide. The author has an hindex of 20, co-authored 38 publications receiving 1657 citations. Previous affiliations of Seiichi Takasaki include Institute of Medical Science.

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Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells

TL;DR: It is proved, for the first time, that recombinant technique can produce glycoprotein hormone whose carbohydrate structures are common to the major sugar chains of the native one.
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Comparative study of the asparagine-linked sugar chains of natural human interferon-beta 1 and recombinant human interferon-beta 1 produced by three different mammalian cells.

TL;DR: The sugar chains of the recombinant interferon-beta 1 derived from Chinese hamster ovary cells were very similar to those of its natural counterpart, in contrast, two other recombinant proteins contain quite different sugar chains.
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Role of sugar chains in the in vitro biological activity of human erythropoietin produced in recombinant Chinese hamster ovary cells.

TL;DR: The results indicate that the core portion of the Asn-type sugar chains is necessary for erythropoietin to express its full biological activity in vitro and suggest that removal of the core portions of the sugar chains destroys the active conformation of erythroietin.
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4-O-Acetyl-N-acetylneuraminic acid in the N-linked carbohydrate structures of equine and guinea pig α2-macroglobulins, potent inhibitors of influenza virus infection

TL;DR: To investigate the molecular basis of the differential ability of human, equine, and guinea pig alpha 2-macroglobulins to inhibit hemagglutination and infectivity of a human influenza virus, A/Memphis/102/72 (H3N2), the structures of oligosaccharides released from the three glycoproteins by hydrazinolysis were analyzed comparatively.
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Impaired selectin-ligand biosynthesis and reduced inflammatory responses in β-1,4-galactosyltransferase-I–deficient mice

TL;DR: It is demonstrated that beta4GalT-I is a major galactosyltransferase responsible for selectin-ligand biosynthesis and that inflammatory responses of beta4 galactose residues in beta-1,4 linkage-deficient mice are impaired because of the defect in selectIn-ligands biosynthesis.