α,2,8-sialyltransferase

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid

Reexamination Certificate

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C435S320100, C435S440000, C435S091400, C435S193000, C435S325000, C435S252300, C435S252330, C536S023200

Reexamination Certificate

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10430325

ABSTRACT:
The invention provides a novel α-2,8-sialyltransferase expressed by a gene cloned from animal cells, a cDNA coding for the α-2,8-sialyltransferase, a method of detecting, or suppressing the production of α-2,8-sialyltransferase by using the cDNA, a recombinant vector containing the DNA as an insert and cells harboring the recombinant vector as well as methods of preparing same. The α-2,8-sialyltransferase of the invention is useful, for example, in the production of carbohydrate chains having a useful physiological activity, for example the ganglioside GD3, and modifications thereof.

REFERENCES:
patent: 5324663 (1994-06-01), Lowe
S. Ohta et al. “Antitumor Effects of a Novel Monoclonl Antibody With high Binding Affinity to Ganglioside GD3”, Cancer Immunol. Immunother. 36: 260-266. (1993).
Yoshida, et al., The Journal of Biological Chemistry, vol. 270, No. 24, Issue of Jun. 16, pp. 14628-14633, 1996, Molecular Cloning of Siaα2,3GalβI,4GlcNAc α2,8-Sialyltransferase from Mouse Brain.
Paulson, et al., The Journal of Biological Chemistry, vol. 252, No. 7, Issue of Apr. 10, pp. 2356-2362, 1977, Purification of Sialyltransferase from Bovine Colostrum by Affinity Chromatography on CDP-agarose.
Weinstein, et al., The Journal of Biological Chemistry, vol. 257, No. 22, Issue of Nov. 25, pp. 13835-13844, 1982, Purification of a Galβl→A4GlcNAc α2→6 Sialyltransferase and a Galβl→3(4)G1cNAc α2→3.
Sadler, et al., The Journal of Biological Chemistry, vol. 254, No. 11, Issue of Jun. 10, pp. 4434-4443, 1979, Purification to Homogeneity of a β-Galactoside α2→3 Sialyltransferase and Partial Purification of an α-N-Acetylgalactosaminide α2→6 Sialyltransferase from Porcine Submaxillary Glands.
Rosenberg, et al., Enzymatic Basis for Increased Expression of GD3 on Human Melanoma Cells Derived from Metastatic Lesions, Journal of Clinical Laboratory Analysis, vol. 2, No. 2, 1988, pp. 91-100.
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Gu, et al., Purification to Homogeneity of GD3 Synthase and Partial Purification of GM3 Synthase From Rat Brain, Biochem. Biophys. Res. Commun. 166(1) 387-383.
Nara, et al., Expression Cloning of a CMP-NeuAc:NeuAcalpha2-3Galbeta 1-4Glcbeta1-1'Ceralpha2,8-Sialyltransferase (GD3 Synthase) From Human Melanoma Cells), Proc. Natl. Acad. Sci. 91(17) 7952-7956 (Aug. 1994).
Sasaki, et al., Expression Cloning of a GM3-Specific Alpha-2,8-Sialyltransferase (GD3 Synthase), J. Biol. Chem. 269(22) 15950-15956 (Jun. 1994).
Haraguchi, et al., Isolation of GD3 Synthase Gene by Expression Cloning of GM3 Alpha-2,8-Sialyltransferase cDNA Using Anti-GD2 Monoclonal Antibody, Proc. Natl. Acad. Sci. 91(22)10455-10459 (Oct. 1994).
Grundmann, et al., Complete cDNA Sequence Encoding Human β-Galatoside Alpha-2,6-Sialyltransferase, Nuc. Acids Res. 18(3) 667 (1990).
Agostaro, et al., Cloning of cDNA Encoding the Membrane-Bound Form of Bovine β1,4-Galactosyltransferase, Eur. J. Biochem. 183: 211-217 (1989).
Sakar, et al., Molecular Cloning and Expression of cDNA Encoding the Enzyme that Controls Conversion of High-Mannose to Hybrid and Complex N-glycans: UDP-N-Acetylglucosamine: Alpha-3-D-Mannoside β-1,2-N-Acetyglucosaminyltransferase 1, PNAS 88: 234-238 (Jan. 1991).
Sadler, et al., JBC, vol. 254, No. 13, Jul. 10, pp. 5934-5941, 1979 Purification to homogeneity and Enzymatic Characterization of an α-N-Acetylgalactosaminide α2→6 Sialyltransferase from Porcine Submaxillary Glands.
Yamashiro et al (Cancer Research 53:5395-5400 (1993)).
Weisgerber (Glycobiology 1(4):357-365 (1991)).

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