1. Hz and H. , 93 (dd, J 9,9' = 12, p.72643

1. Hz, 09 (dd, 1H, H-3a), pp.97-98

. Et-le-thioacétate-de-potassium, 27 g, 2.39 mmol, 1.2 éq.). Le mélange réactionnel est agité vigoureusement pendant 45 min à température ambiante

O. Aco and C. , Me SAc AcHN AcO AcO OAc -suivi de la réaction de couplage entre le fluorure d'?-lactosyle et le N I acétylchitobiose, p.25

L. and L. Ont-Été-effectuées-avec-la-même-colonne, Le système HPLC utilisé est composé d'un système de deux pompes (Beckmann, de type System Gold LC-125S Solvent Module) et d'un injecteur avec une boucle de 20 µL

. Dans-le-cas-de-l, hydrolyse du tétrasaccharide 34, le milieu réactionnel est composé de 160 µL d'une solution du tétrasaccharide 34 (12.6 mg/mL) à laquelle sont ajoutés 40 µL d'une solution de l'enzyme Cel 7B d'H. insolens (1 mg/mL)

R. Kobata and A. , Structures and functions of the sugar chains of glycoproteins, European Journal of Biochemistry, vol.145, issue.2, pp.483-501, 1992.
DOI : 10.1016/0092-8674(90)90444-J

R. Apweiler, H. Hermjakob, and N. Sharon, On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1473, issue.1, pp.4-8, 1999.
DOI : 10.1016/S0304-4165(99)00165-8

P. G. Johansen, R. D. Marshall, and A. Neuberger, Carbohydrates in protein. 3. The preparation and some of the properties of a glycopeptide from hen's-egg albumin, Biochemical Journal, vol.78, issue.3, pp.518-527, 1961.
DOI : 10.1042/bj0780518

P. Sears and C. H. Wong, Enzyme action in glycoprotein synthesis, Cellular and Molecular Life Sciences CMLS, vol.54, issue.3, pp.223-252, 1998.
DOI : 10.1007/s000180050146

L. W. Cunningham, R. W. Clouse, and J. D. Ford, Heterogeneity of the carbohydrate moiety of crystalline ovalbumin, Biochimica et Biophysica Acta, vol.78, issue.2, pp.379-381, 1963.
DOI : 10.1016/0006-3002(63)91652-4

S. C. Hubbard and R. J. Ivatt, Synthesis and Processing of Asparagine-Linked Oligosaccharides, Annual Review of Biochemistry, vol.50, issue.1, pp.555-583, 1981.
DOI : 10.1146/annurev.bi.50.070181.003011

C. Abeijon and C. B. Hirschberg, Topography of glycosylation reactions in the endoplasmic reticulum, Trends in Biochemical Sciences, vol.17, issue.1, pp.32-36, 1992.
DOI : 10.1016/0968-0004(92)90424-8

B. Imperiali and K. L. Shannon, Differences between Asn-Xaa-Thr-containing peptides: a comparison of solution conformation and substrate behavior with oligosaccharyltransferase, Biochemistry, vol.30, issue.18, pp.4374-4380, 1991.
DOI : 10.1021/bi00232a002

B. Imperiali, K. L. Shannon, M. Unno, and K. W. Rickert, Mechanistic proposal for asparagine-linked glycosylation, Journal of the American Chemical Society, vol.114, issue.20, pp.7944-7945, 1992.
DOI : 10.1021/ja00046a069

E. Bause, -glycosylation of proteins, Biochemical Society Transactions, vol.12, issue.3, pp.514-517, 1984.
DOI : 10.1042/bst0120514
URL : https://hal.archives-ouvertes.fr/hal-01283026

E. Bause, W. Breuer, and S. Peters, Investigation of the active site of oligosaccharyltransferase from pig liver using synthetic tripeptides as tools, Biochemical Journal, vol.312, issue.3, pp.979-985, 1995.
DOI : 10.1042/bj3120979

P. Van-den-steen, P. M. Rudd, R. A. Dwek, and G. Opdenakker, Concepts and Principles of O-Linked Glycosylation, Critical Reviews in Biochemistry and Molecular Biology, vol.30, issue.3, pp.151-208, 1998.
DOI : 10.1089/thy.1995.5.425

E. S. Trombetta and A. Helenius, Lectins as chaperones in glycoprotein folding, Current Opinion in Structural Biology, vol.8, issue.5, pp.587-592, 1998.
DOI : 10.1016/S0959-440X(98)80148-6

E. S. Trombetta and A. Helenius, Conformational Requirements for Glycoprotein Reglucosylation in the Endoplasmic Reticulum, The Journal of Cell Biology, vol.267, issue.6, pp.1123-1129, 2000.
DOI : 10.1126/science.272.5268.1606

N. Bruneau, A. Nganga, E. A. Fisher, and D. Lombardo, O-Glycosylation of C-terminal Tandem-repeated Sequences Regulates the Secretion of Rat Pancreatic Bile Salt-dependent Lipase, Journal of Biological Chemistry, vol.272, issue.43, pp.27353-27361, 1997.
DOI : 10.1074/jbc.272.43.27353

P. Van-den-steen, P. M. Rudd, P. Proost, E. Martens, L. Paemen et al., Oligosaccharides of recombinant mouse gelatinase B variants, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1425, issue.3, pp.587-598, 1998.
DOI : 10.1016/S0304-4165(98)00113-5

E. Martin-rendon and D. Blake, Protein glycosylation in disease: new insights into the congenital muscular dystrophies, Trends in Pharmacological Sciences, vol.24, issue.4, pp.178-183, 2003.
DOI : 10.1016/S0165-6147(03)00050-6

H. Schachter, Congenital disorders involving defective N-glycosylation of proteins, Cellular and Molecular Life Sciences, vol.58, issue.8, pp.1085-1104, 2001.
DOI : 10.1007/PL00000923

N. A. Meanwell and M. Krystal, Taking aim at a moving target ??? inhibitors of influenza virus Part 2: viral replication, packaging and release, Drug Discovery Today, vol.1, issue.9, pp.388-397, 1996.
DOI : 10.1016/1359-6446(96)10035-0

T. Boren, P. Falk, K. A. Roth, G. Larson, and S. Normark, Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens, Science, vol.262, issue.5141, pp.1892-1895, 1993.
DOI : 10.1126/science.8018146

S. Linn and W. Arber, Host specificity of DNA produced by Escherichia coli, X. In vitro restriction of phage fd replicative form., Proceedings of the National Academy of Sciences, vol.59, issue.4, pp.1300-1306, 1968.
DOI : 10.1073/pnas.59.4.1300

A. M. Maxam and W. Gilbert, A new method for sequencing DNA., Proceedings of the National Academy of Sciences, vol.74, issue.2, pp.560-564, 1977.
DOI : 10.1073/pnas.74.2.560

F. Sanger and A. R. Coulson, A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase, Journal of Molecular Biology, vol.94, issue.3, pp.441-448, 1975.
DOI : 10.1016/0022-2836(75)90213-2

F. Sanger, S. Nicklen, and A. R. Coulson, DNA sequencing with chain-terminating inhibitors, Proceedings of the National Academy of Sciences, vol.74, issue.12, pp.5463-5467, 1977.
DOI : 10.1073/pnas.74.12.5463

J. R. Swartz, Advances in Escherichia coli production of therapeutic proteins, Current Opinion in Biotechnology, vol.12, issue.2, pp.195-201, 2001.
DOI : 10.1016/S0958-1669(00)00199-3

D. C. Andersen and L. Krummen, Recombinant protein expression for therapeutic applications, Current Opinion in Biotechnology, vol.13, issue.2, pp.117-123, 2002.
DOI : 10.1016/S0958-1669(02)00300-2

F. Baneyx, Recombinant protein expression in Escherichia coli, Current Opinion in Biotechnology, vol.10, issue.5, pp.411-421, 1999.
DOI : 10.1016/S0958-1669(99)00003-8

G. P. Cereghino, J. L. Cereghino, C. Ilgen, and J. M. Cregg, Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris, Current Opinion in Biotechnology, vol.13, issue.4, pp.329-332, 2002.
DOI : 10.1016/S0958-1669(02)00330-0

W. Tanner and L. Lehle, Protein glycosylation in yeast, Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, vol.906, issue.1, pp.81-99, 1987.
DOI : 10.1016/0304-4157(87)90006-2

J. W. Larrick and D. W. Thomas, Producing proteins in transgenic plants and animals, Current Opinion in Biotechnology, vol.12, issue.4, pp.411-418, 2001.
DOI : 10.1016/S0958-1669(00)00236-6

J. K. Ma, P. M. Drake, and P. Christou, Genetic modification: The production of recombinant pharmaceutical proteins in plants, Nature Reviews Genetics, vol.83, issue.10, pp.794-805, 2003.
DOI : 10.1038/nrg1177

R. Fischer, E. Stoger, S. Schillberg, P. Christou, and R. M. Twyman, Plant-based production of biopharmaceuticals, Current Opinion in Plant Biology, vol.7, issue.2, pp.152-158, 2004.
DOI : 10.1016/j.pbi.2004.01.007

P. Lerouge, M. Bardor, S. Pagny, V. Gomord, and L. Faye, N-Glycosylation of Recombinant Pharmaceutical Glycoproteins Produced in Transgenic Plants Towards an Humanisation of Plant N-Glycans, Current Pharmaceutical Biotechnology, vol.1, issue.4, pp.347-354, 2000.
DOI : 10.2174/1389201003378843

N. Jenkins and E. M. Curling, Glycosylation of recombinant proteins: Problems and prospects, Enzyme and Microbial Technology, vol.16, issue.5, pp.354-364, 1994.
DOI : 10.1016/0141-0229(94)90149-X

N. Jenkins, R. Paekh, and D. C. James, Getting the glycosylation right: Implications for the biotechnology industry, Nature Biotechnology, vol.5, issue.8, pp.975-981, 1996.
DOI : 10.1016/S0040-4039(00)93387-2

G. Ashwell and J. Harford, Carbohydrate-Specific Receptors of the Liver, Annual Review of Biochemistry, vol.51, issue.1, pp.531-554, 1982.
DOI : 10.1146/annurev.bi.51.070182.002531

B. G. Davis, Synthesis of Glycoproteins, Chemical Reviews, vol.102, issue.2, pp.579-601, 2002.
DOI : 10.1021/cr0004310

N. J. Davis and S. L. Flitsch, A novel method for the specific glycosylation of proteins, Tetrahedron Letters, vol.32, issue.46, pp.6793-6796, 1991.
DOI : 10.1016/S0040-4039(00)93605-0

S. Y. Wong, G. R. Guile, R. A. Dwek, and G. Arsequell, -saccharide) iodoacetamides: applications in site-specific glycosylation and solid-phase enzymic oligosaccharide synthesis, Biochemical Journal, vol.300, issue.3, pp.843-850, 1994.
DOI : 10.1042/bj3000843
URL : https://hal.archives-ouvertes.fr/hal-00309348

B. G. Davis, M. A. Maughan, M. P. Green, A. Ullman, and J. B. Jones, Glycomethanethiosulfonates: powerful reagents for protein glycosylation, Tetrahedron: Asymmetry, vol.11, issue.1, pp.245-262, 2000.
DOI : 10.1016/S0957-4166(99)00497-8

D. P. Gamblin, P. Garnier, S. J. Ward, N. J. Oldham, A. J. Fairbanks et al., Glycosyl phenylthiosulfonates (Glyco-PTS): novel reagents for glycoprotein synthesisThis is one of a number of contributions from the current members of the Dyson Perrins Laboratory to mark the end of almost 90 years of organic chemistry research in that building, as all its current academic staff move across South Parks Road to a new purpose-built laboratory.Electronic supplementary information (ESI) available: experimental procedures, characterization, protein ESI-MS spectra and crystal data. See http://www.rsc.org/suppdata/ob/b3/b306990g/, Organic & Biomolecular Chemistry, vol.1, issue.21, pp.3642-3644, 2003.
DOI : 10.1039/b306990g

D. P. Gamblin, P. Garnier, S. Van-kasteren, N. J. Oldham, A. J. Fairbanks et al., Glyco-SeS: Selenenylsulfide-Mediated Protein Glycoconjugation???A New Strategy in Post-Translational Modification, Angewandte Chemie International Edition, vol.43, issue.7, pp.828-833, 2004.
DOI : 10.1002/anie.200352975

E. C. Rodriguez, L. A. Marcaurelle, and C. R. Bertozzi, Aminooxy-, Hydrazide-, and Thiosemicarbazide-Functionalized Saccharides:?? Versatile Reagents for Glycoconjugate Synthesis, The Journal of Organic Chemistry, vol.63, issue.21, pp.7134-7135, 1998.
DOI : 10.1021/jo981351n

J. Ni, S. Singh, and L. Wang, Synthesis of Maleimide-Activated Carbohydrates as Chemoselective Tags for Site-Specific Glycosylation of Peptides and Proteins, Bioconjugate Chemistry, vol.14, issue.1, pp.232-238, 2003.
DOI : 10.1021/bc025617f

H. Liu, L. Wang, A. Brock, C. Wong, and P. G. Schultz, A Method for the Generation of Glycoprotein Mimetics, Journal of the American Chemical Society, vol.125, issue.7, pp.1702-1703, 2003.
DOI : 10.1021/ja029433n

K. Witte, P. Sears, and C. Wong, Enzymatic Glycoprotein Synthesis:?? Preparation of Ribonuclease Glycoforms via Enzymatic Glycopeptide Condensation and Glycosylation, Journal of the American Chemical Society, vol.119, issue.9, pp.2114-2118, 1997.
DOI : 10.1021/ja961846z

J. R. Jacobsen and C. Khosla, New directions in metabolic engineering, Current Opinion in Chemical Biology, vol.2, issue.1, pp.133-137, 1998.
DOI : 10.1016/S1367-5931(98)80045-8

G. Stephanopoulos, Metabolic engineering, Current Opinion in Biotechnology, vol.5, issue.2, pp.196-200, 1994.
DOI : 10.1016/S0958-1669(05)80036-9

D. C. Cameron and I. T. Tong, Cellular and metabolic engineering, Applied Biochemistry and Biotechnology, vol.9, issue.35, pp.105-140, 1993.
DOI : 10.1007/BF02916416

S. K. Roy, Y. Chiba, and Y. Jigami, Production of therapeutic glycoproteins through the engineering of glycosylation pathway in yeast, Biotechnology and Bioprocess Engineering, vol.9, issue.4, pp.219-226, 2000.
DOI : 10.1007/BF02942177

R. K. Bretthauer, Genetic engineering of Pichia pastoris to humanize N-glycosylation of proteins, Trends in Biotechnology, vol.21, issue.11, pp.459-462, 2003.
DOI : 10.1016/j.tibtech.2003.09.005

W. Vervecken, V. Kaigorodov, N. Callewaert, S. Geysens, K. De-vusser et al., In Vivo Synthesis of Mammalian-Like, Hybrid-Type N-Glycans in Pichia pastoris, Applied and Environmental Microbiology, vol.70, issue.5, pp.2639-2646, 2004.
DOI : 10.1128/AEM.70.5.2639-2646.2004

D. L. Jarvis, Z. S. Kawar, and J. R. Hollister, Engineering N-glycosylation pathways in the baculovirus-insect cell system, Current Opinion in Biotechnology, vol.9, issue.5, pp.528-533, 1998.
DOI : 10.1016/S0958-1669(98)80041-4

V. Gomord and L. Faye, Posttranslational modification of therapeutic proteins in plants, Current Opinion in Plant Biology, vol.7, issue.2, pp.171-181, 2004.
DOI : 10.1016/j.pbi.2004.01.015

B. Henrissat, A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochemical Journal, vol.280, issue.2, pp.309-316, 1991.
DOI : 10.1042/bj2800309
URL : https://hal.archives-ouvertes.fr/hal-00310263

L. Lemesle-varloot, B. Henrissat, C. Gaboriaud, V. Bissery, and A. Morgat, Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences, Biochimie, vol.72, issue.8, pp.555-574, 1990.
DOI : 10.1016/0300-9084(90)90120-6
URL : https://hal.archives-ouvertes.fr/hal-00310194

G. Davies and B. Henrissat, Structures and mechanisms of glycosyl hydrolases, Structure, vol.3, issue.9, pp.853-859, 1995.
DOI : 10.1016/S0969-2126(01)00220-9
URL : https://hal.archives-ouvertes.fr/hal-00310748

B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J. Mornon et al., Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases., Proceedings of the National Academy of Sciences, vol.92, issue.15, pp.7090-7094, 1995.
DOI : 10.1073/pnas.92.15.7090
URL : https://hal.archives-ouvertes.fr/hal-00310754

B. Henrissat and A. Bairoch, New families in the classification of glycosyl hydrolases based on amino acid sequence similarities, Biochemical Journal, vol.293, issue.3, pp.781-788, 1993.
DOI : 10.1042/bj2930781
URL : https://hal.archives-ouvertes.fr/hal-00310595

B. Henrissat and A. Bairoch, Updating the sequence-based classification of glycosyl hydrolases, Biochemical Journal, vol.316, issue.2, pp.695-696, 1996.
DOI : 10.1042/bj3160695
URL : https://hal.archives-ouvertes.fr/hal-00310822

C. S. Rye and S. G. Withers, Glycosidase mechanisms, Current Opinion in Chemical Biology, vol.4, issue.5, pp.573-580, 2000.
DOI : 10.1016/S1367-5931(00)00135-6

V. L. Yip and S. G. Withers, Nature's many mechanisms for the degradation of oligosaccharides, Organic & Biomolecular Chemistry, vol.2, issue.19, pp.2707-2713, 2004.
DOI : 10.1039/b408880h

D. E. Koshland and . Jr, STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS, Biological Reviews, vol.190, issue.4, pp.416-436, 1953.
DOI : 10.1021/ja01153a012

M. L. Sinnott, Catalytic mechanism of enzymic glycosyl transfer, Chemical Reviews, vol.90, issue.7, pp.1171-1202, 1990.
DOI : 10.1021/cr00105a006

J. D. Mccarter and S. G. Withers, Mechanisms of enzymatic glycoside hydrolysis, Current Opinion in Structural Biology, vol.4, issue.6, pp.885-892, 1994.
DOI : 10.1016/0959-440X(94)90271-2

Q. Wang, R. W. Graham, D. Trimbur, R. A. Warren, and S. G. Withers, Changing Enzymic Reaction Mechanisms by Mutagenesis: Conversion of a Retaining Glucosidase to an Inverting Enzyme, Journal of the American Chemical Society, vol.116, issue.25, pp.11594-11595, 1994.
DOI : 10.1021/ja00104a060

B. Henrissat and G. Davies, Structural and sequence-based classification of glycoside hydrolases, Current Opinion in Structural Biology, vol.7, issue.5, pp.637-644, 1997.
DOI : 10.1016/S0959-440X(97)80072-3
URL : https://hal.archives-ouvertes.fr/hal-00309861

S. G. Withers, L. Mackenzie, Q. Wang, . Withers, and G. Stephen, Methods and compositions for synthesis of oligosaccharides using mutant glycosidase enzymes (The University of British Columbia, Can

L. F. Mackenzie, Q. Wang, R. A. Warren, and S. G. Withers, Glycosynthases:?? Mutant Glycosidases for Oligosaccharide Synthesis, Journal of the American Chemical Society, vol.120, issue.22, pp.5583-5584, 1998.
DOI : 10.1021/ja980833d

H. Prade, L. F. Mackenzie, and S. G. Withers, Enzymatic synthesis of disaccharides using Agrobacterium sp. ??-glucosidase, Carbohydrate Research, vol.305, issue.3-4, pp.371-381, 1998.
DOI : 10.1016/S0008-6215(97)10040-4

G. Perugino, A. Trincone, M. Rossi, and M. Moracci, Oligosaccharide synthesis by glycosynthases, Trends in Biotechnology, vol.22, issue.1, pp.31-37, 2004.
DOI : 10.1016/j.tibtech.2003.10.008

C. Mayer, D. L. Jakeman, M. Mah, G. Karjala, L. Gal et al., Directed evolution of new glycosynthases from Agrobacterium ??-glucosidase: a general screen to detect enzymes for oligosaccharide synthesis, Chemistry & Biology, vol.8, issue.5, pp.437-443, 2001.
DOI : 10.1016/S1074-5521(01)00022-9

M. Okuyama, H. Mori, K. Watanabe, A. Kimura, and S. Chiba, ??-Glucosidase Mutant Catalyzes ?????-Glycosynthase???-type Reaction, Bioscience, Biotechnology, and Biochemistry, vol.51, issue.8, pp.928-933, 2002.
DOI : 10.1271/bbb.65.2657

M. Hrmova, T. Imai, S. J. Rutten, J. K. Fairweather, L. Pelosi et al., Mutated Barley (1,3)-beta -D-Glucan Endohydrolases Synthesize Crystalline (1,3)-beta -D-Glucans, Journal of Biological Chemistry, vol.277, issue.33, pp.30102-30111, 2002.
DOI : 10.1074/jbc.M203971200

J. F. Tolborg, L. Petersen, K. J. Jensen, C. Mayer, D. L. Jakeman et al., Solid-Phase Oligosaccharide and Glycopeptide Synthesis Using Glycosynthases, The Journal of Organic Chemistry, vol.67, issue.12, pp.4143-4149, 2002.
DOI : 10.1021/jo0163445

A. Trincone, G. Perugino, M. Rossi, and M. Moracci, A novel thermophilic Glycosynthase that effects branching glycosylation, Bioorganic & Medicinal Chemistry Letters, vol.10, issue.4, pp.365-368, 2000.
DOI : 10.1016/S0960-894X(99)00700-3

M. Moracci, A. Trincone, B. Cobucci-ponzano, G. Perugino, M. Ciaramella et al., Enzymatic synthesis of oligosaccharides by two glycosyl hydrolases of Sulfolobus solfataricus, Extremophiles, vol.5, issue.3, pp.145-152, 2001.
DOI : 10.1007/s007920100186

A. Trincone, A. Giordano, G. Perugino, M. Rossi, and M. Moracci, Glycosynthase-Catalysed syntheses at pH below neutrality, Bioorganic & Medicinal Chemistry Letters, vol.13, issue.22, pp.4039-4042, 2003.
DOI : 10.1016/j.bmcl.2003.08.037

O. Nashiru, D. L. Zechel, D. Stoll, T. Mohammadzadeh, R. A. Warren et al., ??-Mannosynthase: Synthesis of??-Mannosides with a Mutant??-Mannosidase, Angewandte Chemie International Edition, vol.73, issue.2, pp.417-420, 2001.
DOI : 10.1002/1521-3773(20010119)40:2<417::AID-ANIE417>3.0.CO;2-V

D. L. Jakeman and S. G. Withers, On expanding the repertoire of glycosynthases: Mutant ??-galactosidases forming ??-(1,6)-linkages, Canadian Journal of Chemistry, vol.80, issue.8, pp.866-870, 2002.
DOI : 10.1139/v02-077

S. Fort, V. Boyer, L. Greffe, G. J. Davies, O. Moroz et al., Highly Efficient Synthesis of ??(1 ??? 4)-Oligo- and -Polysaccharides Using a Mutant Cellulase, Journal of the American Chemical Society, vol.122, issue.23, pp.5429-5437, 2000.
DOI : 10.1021/ja9936520
URL : https://hal.archives-ouvertes.fr/hal-00309653

J. K. Fairweather, M. Hrmova, S. J. Rutten, G. B. Fincher, and H. Driguez, Synthesis of Complex Oligosaccharides by Using a Mutated (1,3)--D-Glucan Endohydrolase from Barley, Chemistry - A European Journal, vol.9, issue.11, pp.2603-2610, 2003.
DOI : 10.1002/chem.200304733

M. Jahn, J. Marles, R. A. Warren, and S. G. Withers, Thioglycoligases: Mutant Glycosidases for Thioglycoside Synthesis, Angewandte Chemie International Edition, vol.42, issue.3, pp.352-354, 2003.
DOI : 10.1002/anie.200390114

M. Jahn and S. G. Withers, New Approaches to Enzymatic Oligosaccharide Synthesis: Glycosynthases and Thioglycoligases, Biocatalysis and Biotransformation, vol.116, issue.866, pp.159-166, 2003.
DOI : 10.1271/bbb.66.928

R. V. Stick, K. A. Stubbs, and A. G. Watts, Modifying the Regioselectivity of Glycosynthase Reactions Through Changes in the Acceptor, Australian Journal of Chemistry, vol.57, issue.8, pp.779-786, 2004.
DOI : 10.1071/CH04025

M. Schulein, Enzymatic properties of cellulases from Humicola insolens, Journal of Biotechnology, vol.57, issue.1-3, pp.71-81, 1997.
DOI : 10.1016/S0168-1656(97)00090-4

G. J. Kleywegt, J. Zou, C. Divne, G. J. Davies, I. Sinning et al., The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 ?? resolution, and a comparison with related enzymes, Journal of Molecular Biology, vol.272, issue.3, pp.383-397, 1997.
DOI : 10.1006/jmbi.1997.1243

G. Davies, S. Tolley, K. Wilson, M. Schulein, H. F. Woldike et al., Crystallization and preliminary X-ray analysis of a fungal endoglucanase I, Journal of Molecular Biology, vol.228, issue.3, pp.970-972, 1992.
DOI : 10.1016/0022-2836(92)90879-O

L. F. Mackenzie, G. Sulzenbacher, C. Divne, T. A. Jones, H. Woldike et al., Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2???? resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate, Biochemical Journal, vol.335, issue.2, pp.409-416, 1998.
DOI : 10.1042/bj3350409

C. Schou, G. Rasmussen, M. B. Kaltoft, B. Henrissat, and M. Schulein, Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases, European Journal of Biochemistry, vol.139, issue.3, pp.947-953, 1993.
DOI : 10.1016/0167-7799(87)90102-8
URL : https://hal.archives-ouvertes.fr/hal-00310593

V. M. Ducros, C. A. Tarling, D. L. Zechel, A. M. Brzozowski, T. P. Frandsen et al., Anatomy of Glycosynthesis, Chemistry & Biology, vol.10, issue.7, pp.619-628, 2003.
DOI : 10.1016/S1074-5521(03)00143-1

S. Fort, L. Christiansen, M. Schulein, S. Cottaz, and H. Driguez, Stepwise synthesis of cellodextrins assisted by a mutant cellulase, Israel Journal of Chemistry, vol.39, issue.3-4, pp.217-221, 2000.
DOI : 10.1560/5NCY-L9K2-JND4-MB6Q
URL : https://hal.archives-ouvertes.fr/hal-00309599

M. Faijes, J. K. Fairweather, H. Driguez, and A. Planas, Oligosaccharide Synthesis by Coupledendo-Glycosynthases of Different Specificity: A Straightforward Preparation of Two Mixed-Linkage Hexasaccharide Substrates of 1,3/1,4-??-Glucanases, Chemistry - A European Journal, vol.37, issue.21, pp.4651-4655, 2001.
DOI : 10.1002/1521-3765(20011105)7:21<4651::AID-CHEM4651>3.0.CO;2-6

V. Boyer, S. Fort, T. P. Frandsen, M. Schulein, S. Cottaz et al., Chemoenzymatic Synthesis of a Bifunctionalized Cellohexaoside as a Specific Substrate for the Sensitive Assay of Cellulase by Fluorescence Quenching, Chemistry - A European Journal, vol.57, issue.6, pp.1389-1394, 2002.
DOI : 10.1002/1521-3765(20020315)8:6<1389::AID-CHEM1389>3.0.CO;2-#

T. M. Penning and J. M. Jez, Enzyme Redesign, Chemical Reviews, vol.101, issue.10, pp.3027-3046, 2001.
DOI : 10.1021/cr000049n

K. A. Powell, S. W. Ramer, S. B. Del-cardayre, W. P. Stemmer, M. B. Tobin et al., Directed Evolution and Biocatalysis, Angewandte Chemie International Edition, vol.40, issue.21, pp.3948-3959, 2001.
DOI : 10.1002/1521-3773(20011105)40:21<3948::AID-ANIE3948>3.0.CO;2-N

J. R. Cherry and A. L. Fidantsef, Directed evolution of industrial enzymes: an update, Current Opinion in Biotechnology, vol.14, issue.4, pp.438-443, 2003.
DOI : 10.1016/S0958-1669(03)00099-5

P. A. Dalby, Optimising enzyme function by directed evolution, Current Opinion in Structural Biology, vol.13, issue.4, pp.500-505, 2003.
DOI : 10.1016/S0959-440X(03)00101-5

J. L. Harris and C. S. Craik, Engineering enzyme specificity, Current Opinion in Chemical Biology, vol.2, issue.1, pp.127-132, 1998.
DOI : 10.1016/S1367-5931(98)80044-6

J. B. Jones and G. Desantis, Toward Understanding and Tailoring the Specificity of Synthetically Useful Enzymes, Accounts of Chemical Research, vol.32, issue.2, pp.99-107, 1999.
DOI : 10.1021/ar960078d

F. Cedrone, A. Menez, and E. Quemeneur, Tailoring new enzyme functions by rational redesign, Current Opinion in Structural Biology, vol.10, issue.4, pp.405-410, 2000.
DOI : 10.1016/S0959-440X(00)00106-8

K. Hult and P. Berglund, Engineered enzymes for improved organic synthesis, Current Opinion in Biotechnology, vol.14, issue.4, pp.395-400, 2003.
DOI : 10.1016/S0958-1669(03)00095-8

B. G. Davis, Chemical modification of biocatalysts, Current Opinion in Biotechnology, vol.14, issue.4, pp.379-386, 2003.
DOI : 10.1016/S0958-1669(03)00098-3

F. A. Quiocho and F. M. Richards, INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A, Proceedings of the National Academy of Sciences, vol.52, issue.3, pp.833-839, 1964.
DOI : 10.1073/pnas.52.3.833

G. Desantis and J. B. Jones, Chemical modification of enzymes for enhanced functionality, Current Opinion in Biotechnology, vol.10, issue.4, pp.324-330, 1999.
DOI : 10.1016/S0958-1669(99)80059-7

S. A. Marshall, G. A. Lazar, A. J. Chirino, and . Desjarlais, Rational design and engineering of therapeutic proteins, Drug Discovery Today, vol.8, issue.5, pp.212-221, 2003.
DOI : 10.1016/S1359-6446(03)02610-2

P. Saviranta, T. Haavisto, P. Rappu, M. Karp, and T. Loevgren, In Vitro Enzymatic Biotinylation of Recombinant Fab Fragments through a Peptide Acceptor Tail, Bioconjugate Chemistry, vol.9, issue.6, pp.725-735, 1998.
DOI : 10.1021/bc9800217

M. M. Ling and B. H. Robinson, Approaches to DNA Mutagenesis: An Overview, Analytical Biochemistry, vol.254, issue.2, pp.157-178, 1997.
DOI : 10.1006/abio.1997.2428

C. J. Noren, S. J. Anthony-cahill, M. C. Griffith, and P. G. Schultz, A general method for site-specific incorporation of unnatural amino acids into proteins, Science, vol.244, issue.4901, pp.182-188, 1989.
DOI : 10.1126/science.2649980

J. D. Bain, E. S. Diala, C. G. Glabe, T. A. Dix, and A. R. Chamberlin, Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide, Journal of the American Chemical Society, vol.111, issue.20, pp.8013-8014, 1989.
DOI : 10.1021/ja00202a052

H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat et al., The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235

B. C. Cunningham and J. A. Wells, High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis, Science, vol.244, issue.4908, pp.1081-1085, 1989.
DOI : 10.1126/science.2471267

W. P. Stemmer, DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution., Proceedings of the National Academy of Sciences, vol.91, issue.22, pp.10747-10751, 1994.
DOI : 10.1073/pnas.91.22.10747

H. Liao, T. Mckenzie, and R. Hageman, Isolation of a thermostable enzyme variant by cloning and selection in a thermophile., Proceedings of the National Academy of Sciences, vol.83, issue.3, pp.576-580, 1986.
DOI : 10.1073/pnas.83.3.576

K. Chen and F. H. Arnold, Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide., Proceedings of the National Academy of Sciences, vol.90, issue.12, pp.5618-5622, 1993.
DOI : 10.1073/pnas.90.12.5618

W. P. Stemmer, Rapid evolution of a protein in vitro by DNA shuffling, Nature, vol.370, issue.6488, pp.389-391, 1994.
DOI : 10.1038/370389a0

J. H. Zhang, G. Dawes, and W. P. Stemmer, Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening, Proceedings of the National Academy of Sciences, vol.246, issue.1, pp.4504-4509, 1997.
DOI : 10.1016/0003-9861(86)90487-X

M. T. Reetz, A. Zonta, K. Schimossek, K. Liebeton, and K. Jaeger, Creation of Enantioselective Biocatalysts for Organic Chemistry by In Vitro Evolution, Angewandte Chemie International Edition in English, vol.36, issue.24, pp.2830-2832, 1998.
DOI : 10.1002/anie.199728301

F. C. Christians and L. A. Loeb, Novel human DNA alkyltransferases obtained by random substitution and genetic selection in bacteria., Proceedings of the National Academy of Sciences, vol.93, issue.12, pp.6124-6128, 1996.
DOI : 10.1073/pnas.93.12.6124

H. Lin and V. W. Cornish, Screening and Selection Methods for Large-Scale Analysis of Protein Function, Angewandte Chemie International Edition, vol.41, issue.23, pp.4402-4425, 2002.
DOI : 10.1002/1521-3773(20021202)41:23<4402::AID-ANIE4402>3.0.CO;2-H

S. E. Deacon, K. Mahmoud, R. K. Spooner, S. J. Firbank, P. F. Knowles et al., Enhanced Fructose Oxidase Activity in a Galactose Oxidase Variant, ChemBioChem, vol.238, issue.7, pp.972-979, 2004.
DOI : 10.1002/cbic.200300810

J. S. Thorson, W. A. Barton, D. Hoffmeister, and C. Albermann, Structure-Based Enzyme Engineering and Its Impact on In Vitro Glycorandomization, ChemBioChem, vol.21, issue.1, pp.16-25, 2004.
DOI : 10.1002/cbic.200300620

S. R. Andrews, S. J. Charnock, J. H. Lakey, G. J. Davies, M. Claeyssens et al., Substrate Specificity in Glycoside Hydrolase Family 10: TYROSINE 87 AND LEUCINE 314 PLAY A PIVOTAL ROLE IN DISCRIMINATING BETWEEN GLUCOSE AND XYLOSE BINDING IN THE PROXIMAL ACTIVE SITE OF PSEUDOMONAS CELLULOSA XYLANASE 10A, Journal of Biological Chemistry, vol.275, issue.30, pp.23027-23033, 2000.
DOI : 10.1074/jbc.M000128200

Y. Kim, S. S. Lee, R. A. Warren, and S. G. Withers, Directed Evolution of a Glycosynthase from Agrobacterium sp. Increases Its Catalytic Activity Dramatically and Expands Its Substrate Repertoire, Journal of Biological Chemistry, vol.279, issue.41, pp.42787-42793, 2004.
DOI : 10.1074/jbc.M406890200

C. Schou, G. Rasmussen, M. Schulein, B. Henrissat, and H. Driguez, 4-Thiocellooligosaccharides : Their Synthesis and use as Inhibitors of Cellulases, Journal of Carbohydrate Chemistry, vol.266, issue.6, pp.743-752, 1993.
DOI : 10.1016/0008-6215(92)84090-F
URL : https://hal.archives-ouvertes.fr/hal-00310602

S. T. Cohen-anisfeld, P. T. Lansbury, and . Jr, A practical, convergent method for glycopeptide synthesis, Journal of the American Chemical Society, vol.115, issue.23, pp.10531-10537, 1993.
DOI : 10.1021/ja00076a010

L. Wang, M. Tang, T. Suzuki, K. Kitajima, Y. Inoue et al., -Glycopeptide and Its Inhibitory Activity toward Glycoamidases, Journal of the American Chemical Society, vol.119, issue.46, pp.11137-11146, 1997.
DOI : 10.1021/ja9712027
URL : https://hal.archives-ouvertes.fr/jpa-00209906

G. Windridge and E. C. Jorgensen, 1-Hydroxybenzotriazole as a racemization-suppressing reagent for the incorporation of im-benzyl-L-histidine into peptides, Journal of the American Chemical Society, vol.93, issue.23, pp.6318-6319, 1971.
DOI : 10.1021/ja00752a081

M. Masuda and T. Shimizu, Synthesis of Novel ??,??-Type 1-Glucosamide and 1-Galactosamide Bolaamphiphiles, Journal of Carbohydrate Chemistry, vol.13, issue.3, pp.405-416, 1998.
DOI : 10.1021/ja01599a051

M. Shiozaki, T. Mochizuki, H. Hanzawa, and H. Haruyama, Synthesis of a tetrahydropyrano[2,3-d]oxazole analogue of trehazolin, Carbohydrate Research, vol.288, pp.99-108, 1996.
DOI : 10.1016/S0008-6215(96)90783-1

S. T. Anisfeld, P. T. Lansbury, and . Jr, A convergent approach to the chemical synthesis of asparagine-linked glycopeptides, The Journal of Organic Chemistry, vol.55, issue.21, pp.5560-5562, 1990.
DOI : 10.1021/jo00308a009

M. Bodanszky and J. Martinez, Side reactions in peptide synthesis. 8. On the phenacyl group in the protection of the .beta.-carboxyl function of aspartyl residues, The Journal of Organic Chemistry, vol.43, issue.15, pp.3071-3073, 1978.
DOI : 10.1021/jo00409a035

M. Bodanszky and S. Natarajan, Side reactions in peptide synthesis. II. Formation of succinimide derivatives from aspartyl residues, The Journal of Organic Chemistry, vol.40, issue.17, pp.2495-2499, 1975.
DOI : 10.1021/jo00905a016

K. Kobayashi, E. Tawada, T. Akaike, and T. Usui, Artificial glycopolypeptide conjugates: simple synthesis of lactose- and N,N???-diacetylchitobiose-substituted poly(l-glutamic acid)s through N-??-glycoside linkages and their interaction with lectins, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1336, issue.2, pp.117-122, 1997.
DOI : 10.1016/S0304-4165(97)00018-4

J. Jünnemann, J. Thiem, and C. Pedersen, Facile synthesis of acetylated glycosyl fluorides derived from di- and tri-saccharides, Carbohydrate Research, vol.249, issue.1, pp.91-94, 1993.
DOI : 10.1016/0008-6215(93)84062-B

G. Excoffier, D. Gagnare, and J. P. Utille, Coupure s??lective par l'hydrazine des groupements ac??tyles anom??res de r??sidus glycosyles ac??tyl??s, Carbohydrate Research, vol.39, issue.2, pp.368-373, 1975.
DOI : 10.1016/S0008-6215(00)86150-9

R. Kuhn, P. Lutz, and D. L. Macdonald, Synthese anomerer Sialins??ure-methylketoside, Chemische Berichte, vol.239, issue.2, pp.611-617, 1966.
DOI : 10.1002/cber.19660990235

R. Roy and C. A. Laferriere, -acetylneuraminic acid, Canadian Journal of Chemistry, vol.68, issue.11, pp.2045-2054, 1990.
DOI : 10.1139/v90-313
URL : https://hal.archives-ouvertes.fr/jpa-00209741

K. Jansson, S. Ahlfors, T. Frejd, J. Kihlberg, G. Magnusson et al., 2-(Trimethylsilyl)ethyl glycosides. 3. Synthesis, anomeric deblocking, and transformation into 1,2-trans 1-O-acyl sugars, The Journal of Organic Chemistry, vol.53, issue.24, pp.5629-5647, 1988.
DOI : 10.1021/jo00259a006

K. P. Kartha, A. Kameyama, M. Kiso, and A. Hasegawa, Synthetic Studies Toward Gangliosides and Their Analogs: Synthesis of Appropriately Protected Core Oligosaccharides as Construction Blocks, Journal of Carbohydrate Chemistry, vol.8, issue.1, pp.145-158, 1989.
DOI : 10.1016/0008-6215(85)85005-9

P. J. Card, Fluorinated carbohydrates. Use of DAST in the synthesis of fluorinated sugars, The Journal of Organic Chemistry, vol.48, issue.3, pp.393-395, 1983.
DOI : 10.1021/jo00151a027

T. K. Lindhorst, C. Braun, and S. G. Withers, Syntheses of 4???-deoxy-??-maltosyl fluoride and 4???-deoxy-??-maltotriosyl fluoride as probes of ??-glucanotransferase mechanisms, Carbohydrate Research, vol.268, issue.1, pp.93-106, 1995.
DOI : 10.1016/0008-6215(94)00317-9

Z. Gan and R. Roy, Sialoside clusters as potential ligands for siglecs (sialoadhesins), Canadian Journal of Chemistry, vol.80, issue.8, pp.908-916, 2002.
DOI : 10.1139/v02-053

J. D. Thompson, D. G. Higgins, and T. Gibson, CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Research, vol.22, issue.22, pp.4673-4680, 1994.
DOI : 10.1093/nar/22.22.4673

P. M. Coutinho, M. K. Dowd, and P. Reilly, Automated docking of isomaltose analogues in the glucoamylase active site, Carbohydrate Research, vol.297, issue.4, pp.309-324, 1997.
DOI : 10.1016/S0008-6215(96)00283-2

P. M. Coutinho, M. K. Dowd, and P. Reilly, Automated docking of glucosyl disaccharides in the glucoamylase active site, Proteins: Structure, Function, and Genetics, vol.288, issue.2, pp.162-173, 1997.
DOI : 10.1002/(SICI)1097-0134(199706)28:2<162::AID-PROT5>3.0.CO;2-H

P. M. Coutinho, M. K. Dowd, and P. Reilly, Automated Docking of ??-(1,4)- and ??-(1,6)-Linked Glucosyl Trisaccharides in the Glucoamylase Active Site, Industrial & Engineering Chemistry Research, vol.37, issue.6, pp.2148-2157, 1998.
DOI : 10.1021/ie9706976

G. M. Morris, D. S. Goodsell, R. S. Halliday, R. Huey, W. E. Hart et al., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, Journal of Computational Chemistry, vol.4, issue.14, pp.1639-1662, 1998.
DOI : 10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B
URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.113.6936

G. Vriend, WHAT IF: A molecular modeling and drug design program, Journal of Molecular Graphics, vol.8, issue.1, pp.52-56, 1990.
DOI : 10.1016/0263-7855(90)80070-V

D. A. Pearlman, D. A. Case, J. W. Caldwell, W. S. Ross, T. E. Cheatham et al., AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules, Computer Physics Communications, vol.91, issue.1-3, pp.1-42, 1995.
DOI : 10.1016/0010-4655(95)00041-D

K. Mazeau, S. Perez, and M. Rinaudo, -Acetyl Group Content on the Conformational Extension of Chitin and Chitosan Chains, Journal of Carbohydrate Chemistry, vol.19, issue.9, pp.1269-1284, 2000.
DOI : 10.1016/S0032-3861(98)00130-X
URL : https://hal.archives-ouvertes.fr/hal-00309425

B. Ramakrishnan and K. Qasba-pradman, Structure-based Design of ??1,4-Galactosyltransferase I (??4Gal-T1) with Equally EfficientN-Acetylgalactosaminyltransferase Activity: POINT MUTATION BROADENS ??4Gal-T1 DONOR SPECIFICITY, Journal of Biological Chemistry, vol.277, issue.23, pp.20833-20839, 2002.
DOI : 10.1074/jbc.M111183200

S. L. Marcus, R. Polakowski, N. O. Seto, E. Leinala, S. Borisova et al., A Single Point Mutation Reverses the Donor Specificity of Human Blood Group B-synthesizing Galactosyltransferase, Journal of Biological Chemistry, vol.278, issue.14, pp.12403-12405, 2003.
DOI : 10.1074/jbc.M212002200

A. Rietsch and J. Beckwith, THE GENETICS OF DISULFIDE BOND METABOLISM, Annual Review of Genetics, vol.32, issue.1, pp.163-184, 1998.
DOI : 10.1146/annurev.genet.32.1.163

D. Penninga, B. A. Van-der-veen, R. M. Knegtel, S. A. Van-hijum, H. J. Rozeboom et al., The Raw Starch Binding Domain of Cyclodextrin Glycosyltransferase from Bacillus circulans Strain 251, Journal of Biological Chemistry, vol.271, issue.51, pp.32777-32784, 1996.
DOI : 10.1074/jbc.271.51.32777

M. E. Penttila, L. Andre, M. Saloheimo, P. Lehtovaara, and J. K. Knowles, Expression of twoTrichoderma reesei endoglucanases in the yeastSaccharomyces cerevisiae, Yeast, vol.33, issue.3, pp.175-185, 1987.
DOI : 10.1002/yea.320030305

P. T. Nyffeler, C. Liang, K. M. Koeller, and C. Wong, The Chemistry of Amine???Azide Interconversion:?? Catalytic Diazotransfer and Regioselective Azide Reduction, Journal of the American Chemical Society, vol.124, issue.36, pp.10773-10778, 2002.
DOI : 10.1021/ja0264605

B. Vauzeilles, B. Dausse, S. Palmier, and J. M. Beau, A one-step ??-selective glycosylation of N-acetyl glucosamine and recombinant chitooligosaccharides, Tetrahedron Letters, vol.42, issue.43, pp.7567-7570, 2001.
DOI : 10.1016/S0040-4039(01)01594-5

W. L. Armarego and D. D. Perrin, Purification of Laboratory Chemicals, 1997.

S. Armand, S. Drouillard, M. Schuelein, B. Henrissat, and H. Driguez, A Bifunctionalized Fluorogenic Tetrasaccharide as a Substrate to Study Cellulases, Journal of Biological Chemistry, vol.272, issue.5, pp.2709-2713, 1997.
DOI : 10.1074/jbc.272.5.2709
URL : https://hal.archives-ouvertes.fr/hal-00309899

N. Baggett and B. Marsden, Reinvestigation of the synthesis of 4-methylcoumarin-7-yl 5-acetamido-3,5-dideoxy-??-d-glycero-d-galacto-2-nonulopyranosidonic acid, a fluorogenic substrate for neuraminidase, Carbohydrate Research, vol.110, issue.1, pp.11-18, 1982.
DOI : 10.1016/0008-6215(82)85022-2

M. N. Sharma and R. Eby, Synthesis and conformational studies of 2-??-chloro, 2-??-fluoro, and 2-??-fluoro derivatives of 2-deoxy-N-acetyl-neuraminic acid, Carbohydrate Research, vol.127, issue.2, pp.201-210, 1984.
DOI : 10.1016/0008-6215(84)85354-9

A. Hasegawa, J. Nakamura, and M. Kiso, -Acetylneuraminic Acid, Journal of Carbohydrate Chemistry, vol.5, issue.1, pp.11-19, 1986.
DOI : 10.1016/0008-6215(84)85141-1
URL : https://hal.archives-ouvertes.fr/in2p3-00260521

A. Hasegawa, M. Morita, Y. Ito, H. Ishida, and M. Kiso, Studies on the Thioglycosides of N-Acetylneuraminic Acid 7: Synthesis of S-(??-Sialyl)-(2???6)-??-D-Hexopyranosyl and -(2???6)-??-D-Lactosyl Ceramides and their Biological Activity, Journal of Carbohydrate Chemistry, vol.2028, issue.4, pp.369-392, 1990.
DOI : 10.1055/s-1977-24270

J. Sambrook, E. F. Fritsch, and T. Maniatis, Molecular Cloning : A Laboratory Manual, 1989.

M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

U. K. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1038/227680a0

H. Lin, H. Tao, and V. W. Cornish, Directed Evolution of a Glycosynthase via Chemical Complementation, Journal of the American Chemical Society, vol.126, issue.46, pp.15051-15059, 2004.
DOI : 10.1021/ja046238v