Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2011-05-03
2011-05-03
Wen, Sharon (Department: 1644)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
C530S387100
Reexamination Certificate
active
07935792
ABSTRACT:
A polypeptide of N-acetylglucosamine-6-O-sulfotransferase and a DNA encoding the peptide are provided. The polypeptide is (a) or (b) below:(a) a polypeptide having the amino acid sequence represented by SEQ ID NO: 2; or(b) a polypeptide which includes an amino acid sequence including substitution, deletion, insertion or transposition of one or a few amino acids in the amino acid sequence of (a) and which has an enzymatic activity to transfer a sulfate group from a sulfate group donor to a hydroxyl group at 6 position of an N-acetylglucosamine residue located at a non-reducing end of an oligosaccharide represented the formula I:in-line-formulae description="In-line Formulae" end="lead"?GlcNAcβ1-3Galβ1-4GlcNAc (I)in-line-formulae description="In-line Formulae" end="tail"?where GlcNAc represents an N-acetyl-glucosamine residue, Gal represents a galactose residue, β 1-3 represents a β 1-3 glycosidic linkage, and β 1-4 represents a β 1-4 glycosidic linkage.
REFERENCES:
Spiro, et al. “Characterization of a Rat Liver Golgi Sulphotransferase Responsible for the 6-O-Sulphation of N-Acetylglucosamine Residues in β-Linkage to Mannose; Role in Assembly of Sialyl-Galactosyl-N-Acetylglucosamine 6-Sulphate Sequence of N-Linked Oligosaccharides,”Biochem. J., vol. 319, pp. 209-216, 1996.
Degroote, et al. “Characterization of N-Acetylglucosamine-6-O-Sulfotransferase from Human Respiratory Mucosa Active on Mucin Carbohydrate Chains,”The Journal of Biological Chemistry, vol. 272, No. 47, pp. 29493-29501, Nov. 21, 1997.
Bowman, et al. “Identification of an N-Acetylglucosamine-6-O-Sulfotransferase Activity Specific to Lymphoid Tissue: An Enzyme with a Possible Role in Lymphocyte Homing,”Chemistry&Biology, vol. 5, pp. 447-460, Aug. 1998.
Uchimura, et al. “Human N-Acetylglucosamine-6-O-Sulfotransferase Involved in the Biosynthesis of 6-Sulfo Sialyl Lewis X: Molecular Cloning, Chromosomal Mapping, and Expression in Various Organs and Tumor Cells,”Journal of Biochemistry, vol. 124, pp. 670-678, 1998.
Uchimura, et al. “Molecular Cloning and Characterization of an N-Acetylglucosamine-6-O-Sulfotransferase,”The Journal of Biological Chemistry, vol. 273, No. 35, pp. 22577-22583, Aug. 28, 1998.
Nakazawa, et al. “Glycosyltransferase and Sulfotransferase Activities in Chick Corneal Stromal Cells before and After In Vitro Culture,”Archives of Biochemistry and Biophysics, vol. 359, No. 2, pp. 269-282, Nov. 15, 1998.
Tsuboi, et al. “6'-Sulfo Sialyl LexBut Not 6-Sulfo Sialyl LexExpressed on the Cell Surface Supports L-Selectin-Mediated Adhesion,”The Journal of Biological Chemistry, vol. 271, No. 44. pp. 27213-27216, Nov. 1996.
Chandrasekaran, et al. “Specificity Analysis of Three Clonal and Five Non-Clonal α1,3-L-Fucosyltransferases with Sulfated, Sialylated, or Fucosylated Synthetic Carbohydrates as Acceptors in Relation to the Assembly of 3′-Sialyl-6′-Sulfo Lewis x (the L-Selectin Ligand) and Related Complex Structures,”Biochemistry, vol. 35, pp. 8925-8933, 1996.
Mitsuoka, et al. “Identification of a Major Carbohydrate Capping Group of the L-Selectin Ligand on High Endothelial Venules in Human Lymph Nodes as 6-Sulfo Sialyl Lewis X,”The Journal of Biological Chemistry, vol. 273, No. 18, pp. 11225-11233, May 1, 1998.
Aichi Prefecture
Knobbe Martens Olson & Bear LLP
Wen Sharon
LandOfFree
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