Abstract
This chapter demonstrates a practical approach to a rather sophisticated multienzymatic one-pot reaction in glycoscience. The first applications using the multienzyme system in glycosylation were mostly targeted to generation or regeneration of the activated glycosyl donors in situ (kinases, phosphorylation sequences).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Augé, C., Mathieu, C., and Merienne, C. (1986) The use of an immobilised cyclic multi-enzyme system to synthesize branched penta-and hexa-saccharides assiciated with blood-group I epitopes. Carbohydr. Res. 151, 147–156.
Thiem, J. and Stangier, P. (1990) Preparative-enzymic formation of cytidine 5′-monophosphosialate by integrated cytidine 5′-triphosphate regeneration. Liebigs Ann. Chem. 1101–1105.
Ichikawa, Y., Shen, G.-J., and Wong, C.-H. (1991) Enzyme-catalyzed synthesis of sialyl oligosaccharide with in situ regeneration of CMP-Sialic acid. J. Am. Chem. Soc. 113, 4698–4700.
Stangier, P., Treder, W., and Thiem, J. (1993) Chemoenzymatic galactosialylation with integrated cofactor regeneration. Glycoconjugate J. 10, 26–33.
Křen, V. and Thiem J. (1995) Multienzyme system for a one-pot synthesis of sialyl T-antigen. Angew. Chem. Int. Ed. Engl. 34, 893–895.
Herrmann, G. F., Ichikawa, Y., Wandrey, C., Gaeta, F. C. A., Paulson, J. C., and Wong, C.-H. (1993) A new multi-enzyme system for one-pot synthesis of sialyl oligosaccharides: Combined use of-galactosidase and α(2,6)-sialyltransferase coupled with regeneration in situ of CMP-sialic acid. Tetrahedron Lett. 34, 3091–3094.
Springer, G. F. (1984) T and Tn, general carcinoma autoantigens. Science 224, 1198–1206.
Prokop, O. and Uhlenbruck, G. (1969) The Thomsen Phenomenon in Human Blood and Serum Groups. MacLaren ⇐p; Sons, London, pp. 102–110.
Uhlenbruck, G., Pardoe, G. I., and Bird, G. W. G. (1969) On the specifity of lectins with a broad agglutination spectrum II. Studies on the nature of the T-antigen and the specific receptors for the lectin of Arachis hypogoea (ground-nut). Z. Immunitätsforsch. Allg. Klin. Immunol. 138, 423–433.
Livingston, P. O. (1992) Construction of cancer vaccines with carbohydrate and protein (peptide) tumor antigens. Curr. Opinion Immunol. 4, 624–629.
Cohen, J. (1993) Cancer vaccines get a shot in the arm. Science 262, 841–843.
Lubineau, A., Augé, C., and Francois, P. (1992) The use of porcine liver (2→3)-α-sialyltransferase in the large scale synthesis of α-NeupAc-(2→3)-β-D-Galp-(1→3)-D-GlcpNAc, the epitope of the tumor-associated carbohydrate antigen CA 50. Carbohydr. Res. 228, 137–144.
Sabesan, S. and Paulson, J. C. (1986) Combined chemical and enzymatic synthesis of sialyloligosaccharides and characterization by 500-MHz 1H and 13C NMR spectroscopy. J. Am. Chem. Soc. 108, 2068–2080.
Ito, Y., Gaudino, J. J., and Paulson, J. C. (1993) Synthesis of bioactive sialosides. Pure Appl. Chem. 65, 753–762.
Lubineau, A. and Bienaymé, H. (1991) Synthesis of 2-acetamido-2-deoxy-3-ortho-β-D-galactopyranose from 2-acetamido-2-deoxy-D-glucose through a trifluoromethylsulfonyl group displacement. Carbohydr. Res. 212, 267–271.
Hedbys, L., Johansson, E., Mosbach, K., and Larsson, P.-O. (1989) Synthesis of 2-acetamido-2-deoxy-3-O-β-D-galactopyranose by the sequential use of β-D-galactosidase from bovine testes and Escherichia coli. Carbohydr. Res. 186, 217–223.
Schauer, R. Wember, M., and Ferreira do Amaral, C. (1972) Synthesis of CMP-glycosides of radioactive N-acetyl, N-glycolyl-, N-acetyl-7-O-acetyl-and N-acetyl-8-O-acetylneuraminic acids by CMP-sialate synthase from bovine submaxillary glands. Hoppe-Seyler’s Z. Physiol. Chem. 353, 883–886.
Augé, C., Fernandez-Fernandez, R., and Gautheron, C. (1990) The use of immobilized glycosyltransferase in the synthesis of sialyloligosaccharides. Carbohydr. Res. 200, 257–268.
Distler, J. J. and Jourdian, G. W. (1973) The purification and properties of β-galactosidase from bovine testes. J. Biol. Chem. 248, 6772–6780.
Kren, V. (1992) Fructosylation of ergot alkaloids by yeast invertase. Biotechnol. Lett. 14, 769–772.
David, S., Augé, C., and Gautheron, C. (1991) Enzymic methods in preparative carbohydrate chemistry. Adv. Carbohydr. Chem. Biochem. 49, 175–237.
Higa, H. H. and Paulson, J. C. (1985) Sialylation of glycoprotein oligosaccharides with N-acetyl, N-glycolyl and N-O-diacetylneuraminic acids. J. Biol. Chem. 260, 8838–8849.
Kean, E. L. and Roseman, S. (1966) CMP-Sialic acid synthetase (cytidine-5′-monophospho-sialic acid synhetase). Methods Enzymol. 8, 208–215.
Kean, E. L. (1972) CMP-Sialic acid synthetase of nuclei. Methods Enzymol. 28, 413–421.
Warren, L. (1959) The biosynthesis of cytidine 5′-monophospho-N-acetylneuraminic acid by an enzyme from Neisseria meningitis. J. Biol. Chem. 234, 1971–1975.
Křen, V. and Thiem, J. (1997) A simple and non-radioactive method for determination of sialyltransferase activity. Biotechnol. Techniques 11, 323–326.
Gillespie, W., Kelm, S., and Paulson, J. C. (1992) Cloning and expression of the Galβ1,3GalNAc α2,3-sialyltransferase. J. Biol. Chem. 267, 21,004–21,010.
Sticher, U., Groβ, H. J., and Brossmer, R. (1988) Purification of α2,6-sialyltransferase from rat liver by dye chromatography. Biochem. J. 253, 577–580.
Sato, T., Omichi, K., and Ikenaka, T. (1988) Simple assay for sialyltransferase activity with a new fluorogenic substrate. J. Biochem. (Tokyo) 104, 18–21.
Harada, H., Ueno, Y., Kamei, M., Ohura, R., Tanabe, N., Uchida, Y., et al. (1989) Rapid assay of β-galactosidase and sialyltransferase by lectin affinity high performance liquid chromatography with fluorescence detection. Biomed. Chromatogr. 1989, 110–113.
Groß, H. J., Sticher, U., and Brossmer, R. (1990) A highly sensitive fluorometric assay for sialyltransferase activity using CMP-9-fluoresceinyl-NeuAc as donor. Anal. Biochem. 186, 127–134.
Groß, H. J. and Brossmer, R. (1991) Characterization of human plasma sialyltransferase using novel fluorometric assay. Clin. Chim. Acta. 197, 237–247.
Mattox, S., Walrath, K., Debbie, C., Smith, D. F., and Cummings, R. D. (1992) A solid-phase assay for the activity of CMPNeuAc:Galβ1-4GlcNAc-R α-2, 6-sialyltransferase. Anal. Biochem. 206, 430–436.
Nakamura, M., Tsunoda, A., and Saito, M. (1991) Radioimmune assay of sialyltransferase and N-acetylgalactosaminyltransferase activities using specific antibodies on a 96-well filtration plate of a multiscreen assay system. Anal. Biochem. 198, 154–159.
Spiegel, L. B., Hadjimichael, J., and Rossomando, E. F. (1992) Assay of sialyltransferase activity by reversed-phase ion-pair high-performance liquid chromatography. J. Chromatogr. 573, 23–27.
Warren, L. (1956) The thiobarbituric acid assay for sialic acid. J. Biol. Chem. 234, 1971–1975.
Gosselin, S., Alhussaini, M., Streiff, M. B., Takabayashi, K., and Palcic, M. M. (1994) A continuous spectrophotometric assay for glycosyltransferases. Anal. Biochem. 220, 92–97.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Křen, V. (1999). One-Pot Enzymatic Synthesis of Sialyl T-Epitope. In: Bucke, C. (eds) Carbohydrate Biotechnology Protocols. Methods in Biotechnology™, vol 10. Humana Press. https://doi.org/10.1007/978-1-59259-261-6_14
Download citation
DOI: https://doi.org/10.1007/978-1-59259-261-6_14
Publisher Name: Humana Press
Print ISBN: 978-0-89603-563-8
Online ISBN: 978-1-59259-261-6
eBook Packages: Springer Protocols