The Experts below are selected from a list of 19305 Experts worldwide ranked by ideXlab platform

Sumihiro Hase - One of the best experts on this subject based on the ideXlab platform.

  • structural analysis of n linked sugar chains of human Blood Clotting factor ix
    Journal of Biochemistry, 2000
    Co-Authors: Yasushi Makino, Kaoru Omichi, Nahoki Kuraya, Hideyuki Ogawa, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    The structures of N-glycans of human Blood Clotting factor IX were studied. N-Glycans liberated by hydrazinolysis were N-acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. Each PA-sugar chain was analyzed by two-dimensional sugar mapping combined with glycosidase digestion. The major structures of the N-linked sugar chains of human factor IX were found to be sialotetraantennary and sialotriantennary chains with or without fucose residues. These highly sialylated sugar chains are located on the activation peptide of the protein.

  • structural analysis of o linked sugar chains in human Blood Clotting factor ix
    Journal of Biochemistry, 1993
    Co-Authors: Nahoki Kuraya, Kaoru Omichi, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    Type and structural analysis of O-linked sugar chains in human Blood Clotting factor IX was performed by the pyridylamination method developed for O-linked sugar chains [Kuraya, N. & Hase, S. (1992) J. Biochem. 112, 122-126]. O- and N-linked sugar chains were released with hydrazine, and then N-acetylated, followed by pyridylamination. The type of sugar chain was determined by reducing-end analysis of the pyridylaminated (PA-) sugar chains. Sugar chains with PA-GalNAc at the reducing terminal and that with PA-Fuc [Nishimura, H. et al. (1992) J. Biol. Chem. 267, 17520-17525] were obtained besides known sugar chains with PA-Glc from the Xyl-Glc-Ser type and those with PA-GlcNAc from asparagine-linked sugar chains. The sugar chains with PA-GalNAc were identified as mono- and disialyl Gal beta 1-3GalNAc by two-dimensional HPLC mapping. The structure of the sugar chain with PA-Fuc was Neu5Ac alpha 2-6Gal beta 1-4GlcNAc beta 1-3Fuc, as determined by exoglycosidase digestion, methylation analysis, and Smith degradation.

Nahoki Kuraya - One of the best experts on this subject based on the ideXlab platform.

  • structural analysis of n linked sugar chains of human Blood Clotting factor ix
    Journal of Biochemistry, 2000
    Co-Authors: Yasushi Makino, Kaoru Omichi, Nahoki Kuraya, Hideyuki Ogawa, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    The structures of N-glycans of human Blood Clotting factor IX were studied. N-Glycans liberated by hydrazinolysis were N-acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. Each PA-sugar chain was analyzed by two-dimensional sugar mapping combined with glycosidase digestion. The major structures of the N-linked sugar chains of human factor IX were found to be sialotetraantennary and sialotriantennary chains with or without fucose residues. These highly sialylated sugar chains are located on the activation peptide of the protein.

  • structural analysis of o linked sugar chains in human Blood Clotting factor ix
    Journal of Biochemistry, 1993
    Co-Authors: Nahoki Kuraya, Kaoru Omichi, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    Type and structural analysis of O-linked sugar chains in human Blood Clotting factor IX was performed by the pyridylamination method developed for O-linked sugar chains [Kuraya, N. & Hase, S. (1992) J. Biochem. 112, 122-126]. O- and N-linked sugar chains were released with hydrazine, and then N-acetylated, followed by pyridylamination. The type of sugar chain was determined by reducing-end analysis of the pyridylaminated (PA-) sugar chains. Sugar chains with PA-GalNAc at the reducing terminal and that with PA-Fuc [Nishimura, H. et al. (1992) J. Biol. Chem. 267, 17520-17525] were obtained besides known sugar chains with PA-Glc from the Xyl-Glc-Ser type and those with PA-GlcNAc from asparagine-linked sugar chains. The sugar chains with PA-GalNAc were identified as mono- and disialyl Gal beta 1-3GalNAc by two-dimensional HPLC mapping. The structure of the sugar chain with PA-Fuc was Neu5Ac alpha 2-6Gal beta 1-4GlcNAc beta 1-3Fuc, as determined by exoglycosidase digestion, methylation analysis, and Smith degradation.

Kaoru Omichi - One of the best experts on this subject based on the ideXlab platform.

  • structural analysis of n linked sugar chains of human Blood Clotting factor ix
    Journal of Biochemistry, 2000
    Co-Authors: Yasushi Makino, Kaoru Omichi, Nahoki Kuraya, Hideyuki Ogawa, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    The structures of N-glycans of human Blood Clotting factor IX were studied. N-Glycans liberated by hydrazinolysis were N-acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. Each PA-sugar chain was analyzed by two-dimensional sugar mapping combined with glycosidase digestion. The major structures of the N-linked sugar chains of human factor IX were found to be sialotetraantennary and sialotriantennary chains with or without fucose residues. These highly sialylated sugar chains are located on the activation peptide of the protein.

  • structural analysis of o linked sugar chains in human Blood Clotting factor ix
    Journal of Biochemistry, 1993
    Co-Authors: Nahoki Kuraya, Kaoru Omichi, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    Type and structural analysis of O-linked sugar chains in human Blood Clotting factor IX was performed by the pyridylamination method developed for O-linked sugar chains [Kuraya, N. & Hase, S. (1992) J. Biochem. 112, 122-126]. O- and N-linked sugar chains were released with hydrazine, and then N-acetylated, followed by pyridylamination. The type of sugar chain was determined by reducing-end analysis of the pyridylaminated (PA-) sugar chains. Sugar chains with PA-GalNAc at the reducing terminal and that with PA-Fuc [Nishimura, H. et al. (1992) J. Biol. Chem. 267, 17520-17525] were obtained besides known sugar chains with PA-Glc from the Xyl-Glc-Ser type and those with PA-GlcNAc from asparagine-linked sugar chains. The sugar chains with PA-GalNAc were identified as mono- and disialyl Gal beta 1-3GalNAc by two-dimensional HPLC mapping. The structure of the sugar chain with PA-Fuc was Neu5Ac alpha 2-6Gal beta 1-4GlcNAc beta 1-3Fuc, as determined by exoglycosidase digestion, methylation analysis, and Smith degradation.

Sadaaki Iwanaga - One of the best experts on this subject based on the ideXlab platform.

  • structural analysis of n linked sugar chains of human Blood Clotting factor ix
    Journal of Biochemistry, 2000
    Co-Authors: Yasushi Makino, Kaoru Omichi, Nahoki Kuraya, Hideyuki Ogawa, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    The structures of N-glycans of human Blood Clotting factor IX were studied. N-Glycans liberated by hydrazinolysis were N-acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. Each PA-sugar chain was analyzed by two-dimensional sugar mapping combined with glycosidase digestion. The major structures of the N-linked sugar chains of human factor IX were found to be sialotetraantennary and sialotriantennary chains with or without fucose residues. These highly sialylated sugar chains are located on the activation peptide of the protein.

  • structural analysis of o linked sugar chains in human Blood Clotting factor ix
    Journal of Biochemistry, 1993
    Co-Authors: Nahoki Kuraya, Kaoru Omichi, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    Type and structural analysis of O-linked sugar chains in human Blood Clotting factor IX was performed by the pyridylamination method developed for O-linked sugar chains [Kuraya, N. & Hase, S. (1992) J. Biochem. 112, 122-126]. O- and N-linked sugar chains were released with hydrazine, and then N-acetylated, followed by pyridylamination. The type of sugar chain was determined by reducing-end analysis of the pyridylaminated (PA-) sugar chains. Sugar chains with PA-GalNAc at the reducing terminal and that with PA-Fuc [Nishimura, H. et al. (1992) J. Biol. Chem. 267, 17520-17525] were obtained besides known sugar chains with PA-Glc from the Xyl-Glc-Ser type and those with PA-GlcNAc from asparagine-linked sugar chains. The sugar chains with PA-GalNAc were identified as mono- and disialyl Gal beta 1-3GalNAc by two-dimensional HPLC mapping. The structure of the sugar chain with PA-Fuc was Neu5Ac alpha 2-6Gal beta 1-4GlcNAc beta 1-3Fuc, as determined by exoglycosidase digestion, methylation analysis, and Smith degradation.

Hitoshi Nishimura - One of the best experts on this subject based on the ideXlab platform.

  • structural analysis of n linked sugar chains of human Blood Clotting factor ix
    Journal of Biochemistry, 2000
    Co-Authors: Yasushi Makino, Kaoru Omichi, Nahoki Kuraya, Hideyuki Ogawa, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    The structures of N-glycans of human Blood Clotting factor IX were studied. N-Glycans liberated by hydrazinolysis were N-acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. Each PA-sugar chain was analyzed by two-dimensional sugar mapping combined with glycosidase digestion. The major structures of the N-linked sugar chains of human factor IX were found to be sialotetraantennary and sialotriantennary chains with or without fucose residues. These highly sialylated sugar chains are located on the activation peptide of the protein.

  • structural analysis of o linked sugar chains in human Blood Clotting factor ix
    Journal of Biochemistry, 1993
    Co-Authors: Nahoki Kuraya, Kaoru Omichi, Hitoshi Nishimura, Sadaaki Iwanaga, Sumihiro Hase
    Abstract:

    Type and structural analysis of O-linked sugar chains in human Blood Clotting factor IX was performed by the pyridylamination method developed for O-linked sugar chains [Kuraya, N. & Hase, S. (1992) J. Biochem. 112, 122-126]. O- and N-linked sugar chains were released with hydrazine, and then N-acetylated, followed by pyridylamination. The type of sugar chain was determined by reducing-end analysis of the pyridylaminated (PA-) sugar chains. Sugar chains with PA-GalNAc at the reducing terminal and that with PA-Fuc [Nishimura, H. et al. (1992) J. Biol. Chem. 267, 17520-17525] were obtained besides known sugar chains with PA-Glc from the Xyl-Glc-Ser type and those with PA-GlcNAc from asparagine-linked sugar chains. The sugar chains with PA-GalNAc were identified as mono- and disialyl Gal beta 1-3GalNAc by two-dimensional HPLC mapping. The structure of the sugar chain with PA-Fuc was Neu5Ac alpha 2-6Gal beta 1-4GlcNAc beta 1-3Fuc, as determined by exoglycosidase digestion, methylation analysis, and Smith degradation.