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Volumn 245, Issue 3, 1997, Pages 617-625

Structural characterization of N-linked oligosaccharides from cellobiohydrolase I secreted by the filamentous fungus Trichoderma reesei RUTC 30

Author keywords

cellobiohydrolase I; fungus; N glycans; NMR; Trichoderma reesei

Indexed keywords

CELLULOSE 1,4 BETA CELLOBIOSIDASE; OLIGOSACCHARIDE;

EID: 0030957795     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00617.x     Document Type: Article
Times cited : (82)

References (55)
  • 1
    • 0028877138 scopus 로고
    • Production of recombinant proteins in the filamentous fungus Trichoderma reesei
    • Keränen, S. & Penttilä. M. (1993) Production of recombinant proteins in the filamentous fungus Trichoderma reesei, Curr. Opin. Biotechnol. 6, 534-537.
    • (1993) Curr. Opin. Biotechnol. , vol.6 , pp. 534-537
    • Keränen, S.1    Penttilä, M.2
  • 2
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implications
    • Cumming, D. A. (1991) Glycosylation of recombinant protein therapeutics: control and functional implications, Glycobiology 1, 115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cumming, D.A.1
  • 3
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer, K. (1988) Two distinct classes of carbohydrate-recognition domains in animal lectins, J. Biol. Chem. 263, 9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 4
    • 0024722096 scopus 로고
    • High levels of circulating neutralizing antibody in normal animals to recombinant mouse interferon-β produced in yeast
    • Sedmak, J. J. & Grossberg, S. E. (1989) High levels of circulating neutralizing antibody in normal animals to recombinant mouse interferon-β produced in yeast, J. Interferon Res. 9, S61-S65.
    • (1989) J. Interferon Res. , vol.9
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 5
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-Å resolution
    • Aleshin, A., Golubev, A., Firsov, L. M. & Honzatko, R. B. (1992) Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-Å resolution, J. Biol. Chem. 267, 19291-19298.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 6
    • 0027524652 scopus 로고
    • The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi
    • Chiba, Y., Yamagata, Y., Iijma, S., Nakajima, T. & Ichishima, E. (1993) The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi, Curr. Microbiol. 27, 281-288.
    • (1993) Curr. Microbiol. , vol.27 , pp. 281-288
    • Chiba, Y.1    Yamagata, Y.2    Iijma, S.3    Nakajima, T.4    Ichishima, E.5
  • 9
    • 0015137704 scopus 로고
    • The complete sequence of a glycopeptide obtained from Taka-amylase A
    • Yamaguchi, H., Ikenaka, T. & Matsushima, Y. (1971) The complete sequence of a glycopeptide obtained from Taka-amylase A, J. Biochem. (Tokyo) 70, 587-594.
    • (1971) J. Biochem. (Tokyo) , vol.70 , pp. 587-594
    • Yamaguchi, H.1    Ikenaka, T.2    Matsushima, Y.3
  • 10
    • 0028393188 scopus 로고
    • Novel structures of N-linked high-mannose type oligosaccharides containing α-D-galactofuranosyl linkages in Aspergillus niger α-D-glucosidase
    • Takayanagi, T., Kimura, A., Chiba, S. & Ajisaka, K. (1994) Novel structures of N-linked high-mannose type oligosaccharides containing α-D-galactofuranosyl linkages in Aspergillus niger α-D-glucosidase, Carbohydr. Res. 256, 149-158.
    • (1994) Carbohydr. Res. , vol.256 , pp. 149-158
    • Takayanagi, T.1    Kimura, A.2    Chiba, S.3    Ajisaka, K.4
  • 12
    • 0023146852 scopus 로고
    • Low molecular mass high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei
    • Salovuori, I., Makarow, M., Rauvala, H., Knowles, J. & Kääriäinen, L. (1987) Low molecular mass high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei, Biotechnology (N. Y.) 5, 152-156.
    • (1987) Biotechnology (N. Y.) , vol.5 , pp. 152-156
    • Salovuori, I.1    Makarow, M.2    Rauvala, H.3    Knowles, J.4    Kääriäinen, L.5
  • 13
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • Moremen, K. W., Trimble, R. B. & Herscovics, A. (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway, Glycobiology 4, 113-125.
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.B.2    Herscovics, A.3
  • 14
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A. & Orlean, P. (1993) Glycoprotein biosynthesis in yeast, FASEB J. 7, 540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 15
    • 0000372094 scopus 로고
    • The primary structure of a 1,4-β-glucan cellobiohydrolase from the fungus Trichoderma reesei QM 9414
    • Fägerstam, L. G., Pettersson, L. G. & Engström, J. Å. (1984) The primary structure of a 1,4-β-glucan cellobiohydrolase from the fungus Trichoderma reesei QM 9414, FEBS Lett. 167, 309-315.
    • (1984) FEBS Lett. , vol.167 , pp. 309-315
    • Fägerstam, L.G.1    Pettersson, L.G.2    Engström, J.Å.3
  • 17
    • 0021050307 scopus 로고
    • Characterization and properties of cellulases purified from Trichoderma reesei strain L27
    • Shoemaker, S., Watt, K., Tsitovsky, G. & Cox, R. (1983) Characterization and properties of cellulases purified from Trichoderma reesei strain L27, Biotechnology (N. Y.) 1, 687-690.
    • (1983) Biotechnology (N. Y.) , vol.1 , pp. 687-690
    • Shoemaker, S.1    Watt, K.2    Tsitovsky, G.3    Cox, R.4
  • 18
  • 19
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino, A. L. & Plummer, T. H. Jr (1994) Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum, Methods Enzymol. 230, 44-57.
    • (1994) Methods Enzymol. , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 20
    • 0003705101 scopus 로고
    • Sequential Endo H and PNGase F deglycosylation of bulk glycoproteins
    • Verostek, M. F., Lubowski, C. & Trimble, R. B. (1992) Sequential Endo H and PNGase F deglycosylation of bulk glycoproteins, Glycobiology 2, 458.
    • (1992) Glycobiology , vol.2 , pp. 458
    • Verostek, M.F.1    Lubowski, C.2    Trimble, R.B.3
  • 21
    • 0028327131 scopus 로고
    • The analysis of fluorophore-labeled glycans by high-resolution polyacrylamide gel electrophoresis
    • Jackson, P. (1994) The analysis of fluorophore-labeled glycans by high-resolution polyacrylamide gel electrophoresis, Anal. Biochem. 216, 243-252.
    • (1994) Anal. Biochem. , vol.216 , pp. 243-252
    • Jackson, P.1
  • 22
    • 0028313979 scopus 로고
    • Size fractionation of oligosaccharides
    • Kobata, A. (1994) Size fractionation of oligosaccharides, Methods Enzymol. 230, 200-208.
    • (1994) Methods Enzymol. , vol.230 , pp. 200-208
    • Kobata, A.1
  • 23
    • 0019463665 scopus 로고
    • Purification of an acidic α-D-mannosidase from Aspergillus saitoi and specific cleavage of 1,2-α-D-mannosidic linkage in yeast mannan
    • Ichishima, E., Arai, M., Shigematsu, Y., Kumagai, H. & Sumida-Tanaka, R. (1981) Purification of an acidic α-D-mannosidase from Aspergillus saitoi and specific cleavage of 1,2-α-D-mannosidic linkage in yeast mannan, Biochim. Biophys. Acta 658, 45-53.
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 45-53
    • Ichishima, E.1    Arai, M.2    Shigematsu, Y.3    Kumagai, H.4    Sumida-Tanaka, R.5
  • 24
    • 0028861654 scopus 로고
    • Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas
    • Wong-Madden, S. T. & Landry, D. (1995) Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas, Glycobiology 5, 19-28.
    • (1995) Glycobiology , vol.5 , pp. 19-28
    • Wong-Madden, S.T.1    Landry, D.2
  • 25
    • 0014199519 scopus 로고
    • Studies on the glycosidases in jack bean meal. I. Isolation and properties of α-mannosidase
    • Li, Y.-T. (1967) Studies on the glycosidases in jack bean meal. I. Isolation and properties of α-mannosidase, J. Biol. Chem. 242, 5474-5480.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5474-5480
    • Li, Y.-T.1
  • 26
    • 0024355993 scopus 로고
    • High-performance liquid chromatography of reducing carbohydrates as strongly ultraviolet-absorbing and electrochemically sensitive 1-phenyl-3-methyl-5-pyrazolone derivatives
    • Honda, S., Akao, E., Suzuki, S., Okuda, M., Kakehi, K. & Nakamura, J. (1989) High-performance liquid chromatography of reducing carbohydrates as strongly ultraviolet-absorbing and electrochemically sensitive 1-phenyl-3-methyl-5-pyrazolone derivatives, Anal. Biochem. 180, 351-357.
    • (1989) Anal. Biochem. , vol.180 , pp. 351-357
    • Honda, S.1    Akao, E.2    Suzuki, S.3    Okuda, M.4    Kakehi, K.5    Nakamura, J.6
  • 27
    • 0028325772 scopus 로고
    • High-pH anion-exchange chromatography of glycoprotein-derived carbohydrates
    • Hardy, M. R. & Townsend, R. R. (1994) High-pH anion-exchange chromatography of glycoprotein-derived carbohydrates, Methods Enzymol. 230, 208-225.
    • (1994) Methods Enzymol. , vol.230 , pp. 208-225
    • Hardy, M.R.1    Townsend, R.R.2
  • 28
    • 0025472501 scopus 로고
    • Separation of yeast asparagine-linked oligosaccharides by high-performance anion-exchange chromatography
    • Hernandez, L. M., Ballou, L. & Ballou, C. E. (1990) Separation of yeast asparagine-linked oligosaccharides by high-performance anion-exchange chromatography, Carbohydr. Res, 203, 1-11.
    • (1990) Carbohydr. Res , vol.203 , pp. 1-11
    • Hernandez, L.M.1    Ballou, L.2    Ballou, C.E.3
  • 29
    • 0023752198 scopus 로고
    • High-performance anion-exchange chromatography of oligosaccharides using pellicular resins and pulsed amperometric detection
    • Townsend, R. R., Hardy, M. R., Hindsgaul, O. & Lee, Y. C. (1988) High-performance anion-exchange chromatography of oligosaccharides using pellicular resins and pulsed amperometric detection, Anal. Biochem. 174, 459-470.
    • (1988) Anal. Biochem. , vol.174 , pp. 459-470
    • Townsend, R.R.1    Hardy, M.R.2    Hindsgaul, O.3    Lee, Y.C.4
  • 30
    • 0028183063 scopus 로고
    • 1H nuclear magnetic resonance spectroscopy of carbohydrate chains of glycoproteins
    • 1H nuclear magnetic resonance spectroscopy of carbohydrate chains of glycoproteins, Methods Enzvmol. 230, 132-168.
    • (1994) Methods Enzvmol. , vol.230 , pp. 132-168
    • Van Halbeek, H.1
  • 31
    • 0343373375 scopus 로고
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins, Adv. Carbohydr. Chem. Biochem. 41, 209-374.
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 209-374
    • Vliegenthart, J.F.G.1    Dorland, L.2    Van Halbeek, H.3
  • 33
    • 0011837976 scopus 로고
    • Nuclear magnetic resonance spectroscopy. Carbon-13 spectra of some inositols and their O-methylated derivatives
    • Dorman, D. E., Angyal, S. J. & Roberts, J. D. (1970) Nuclear magnetic resonance spectroscopy. Carbon-13 spectra of some inositols and their O-methylated derivatives, J. Am. Chem. Soc. 92, 1351-1354.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 1351-1354
    • Dorman, D.E.1    Angyal, S.J.2    Roberts, J.D.3
  • 34
    • 77956834126 scopus 로고
    • Nuclear magnetic resonance spectroscopy in the study of mono- and oligosaccharides
    • Bock, K. & Thøgersen, H. (1982) Nuclear magnetic resonance spectroscopy in the study of mono- and oligosaccharides, Annu. Rep. NMR Spectroscopy 13, 1-57.
    • (1982) Annu. Rep. NMR Spectroscopy , vol.13 , pp. 1-57
    • Bock, K.1    Thøgersen, H.2
  • 35
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A. & Davis, D. G. (1985) Practical aspects of two-dimensional transverse NOE spectroscopy, J. Magn. Reson. 63, 207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 36
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 37
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sørensen, O. W. & Ernst, R. R. (1982) Multiple quantum filters for elucidating NMR coupling networks, J. Am. Chem. Soc. 104, 6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 38
    • 0000329671 scopus 로고
    • Two-dimensional relayed coherence transfer spectroscopy of a protein
    • Wagner, G. (1983) Two-dimensional relayed coherence transfer spectroscopy of a protein, J. Magn. Reson. 55, 151-156.
    • (1983) J. Magn. Reson. , vol.55 , pp. 151-156
    • Wagner, G.1
  • 39
    • 0010520105 scopus 로고
    • Multiple-step relayed correlation spectroscopy: Sequential resonance assignments in oligosaccharides
    • Homans, S. W., Dwek, R. A., Fernandes, D. L. & Rademacher, T. W. (1984) Multiple-step relayed correlation spectroscopy: Sequential resonance assignments in oligosaccharides, Proc. Natl Acad. Sci. USA 81, 6286-6289.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6286-6289
    • Homans, S.W.1    Dwek, R.A.2    Fernandes, D.L.3    Rademacher, T.W.4
  • 40
    • 46149134725 scopus 로고
    • Improvement of dynamic range in NMR by oversampling
    • Delsuc, M. A. & Lallemand, J. Y. (1986) Improvement of dynamic range in NMR by oversampling, J. Magn. Reson. 69, 504-507.
    • (1986) J. Magn. Reson. , vol.69 , pp. 504-507
    • Delsuc, M.A.1    Lallemand, J.Y.2
  • 41
    • 0041045434 scopus 로고
    • Distortionless enhancement of NMR signals by polarization transfer
    • Doddrell, D. M., Pegg, D. T. & Bendall, M. R. (1982) Distortionless enhancement of NMR signals by polarization transfer, J. Magn. Reson. 48, 323-327.
    • (1982) J. Magn. Reson. , vol.48 , pp. 323-327
    • Doddrell, D.M.1    Pegg, D.T.2    Bendall, M.R.3
  • 42
    • 0019035061 scopus 로고
    • Structural study of the carbohydrate moiety of bovine pancreatic ribonuclease B
    • Liang, C.-J., Yamashita, K. & Kobata, A. (1980) Structural study of the carbohydrate moiety of bovine pancreatic ribonuclease B, J. Biochem. (Tokyo) 88, 51-58.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 51-58
    • Liang, C.-J.1    Yamashita, K.2    Kobata, A.3
  • 44
    • 0010285919 scopus 로고
    • Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy
    • Bax, A. & Subramanian, S. (1986) Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy, J. Magn. Reson. 67, 185-189.
    • (1986) J. Magn. Reson. , vol.67 , pp. 185-189
    • Bax, A.1    Subramanian, S.2
  • 45
    • 34547130099 scopus 로고
    • Carbon-13 nuclear magnetic resonance spectroscopy of monosaccharides
    • Bock, K. & Pedersen, C. (1983) Carbon-13 nuclear magnetic resonance spectroscopy of monosaccharides, Adv. Carbohydr. Chem. Biochem. 41, 27-66.
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 27-66
    • Bock, K.1    Pedersen, C.2
  • 46
    • 0001066547 scopus 로고
    • Substitutional and configurational effects on chemical shift in pyranoid carbohydrate derivatives
    • Lemieux, R. U. & Stevens, J. D. (1965) Substitutional and configurational effects on chemical shift in pyranoid carbohydrate derivatives, Can. J. Chem. 43, 2059-2067.
    • (1965) Can. J. Chem. , vol.43 , pp. 2059-2067
    • Lemieux, R.U.1    Stevens, J.D.2
  • 48
    • 84985201137 scopus 로고
    • Bestimmung der Konformationen von Tri- und Tetrasaccharid-Sequenzen der Core-Struktur von N-Glycoproteinen. Problem der (I→6)-glycosidischen Bindung
    • Paulsen, H., Peters, T., Sinnwell, V., Lebuhn, R. & Meyer, B. (1984) Bestimmung der Konformationen von Tri- und Tetrasaccharid-Sequenzen der Core-Struktur von N-Glycoproteinen. Problem der (I→6)-glycosidischen Bindung, Liebigs Ann. Chem. 951-976.
    • (1984) Liebigs Ann. Chem. , pp. 951-976
    • Paulsen, H.1    Peters, T.2    Sinnwell, V.3    Lebuhn, R.4    Meyer, B.5
  • 49
    • 0013271569 scopus 로고
    • Carbon-13 nuclear magnetic resonance data for oligosaccharides
    • Bock, K., Pedersen, C. & Pedersen, H. (1984) Carbon-13 nuclear magnetic resonance data for oligosaccharides, Adv. Carbohydr. Chem. Biochem. 42, 193-225.
    • (1984) Adv. Carbohydr. Chem. Biochem. , vol.42 , pp. 193-225
    • Bock, K.1    Pedersen, C.2    Pedersen, H.3
  • 50
    • 0020396244 scopus 로고
    • Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases
    • Saunier, B., Kilker, R. D. Jr, Tkacz, J. S., Quaroni, A. & Herscovics, A. (1982) Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases, J. Biol. Chem. 257, 14155-14161.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14155-14161
    • Saunier, B.1    Kilker Jr., R.D.2    Tkacz, J.S.3    Quaroni, A.4    Herscovics, A.5
  • 51
    • 0021277449 scopus 로고
    • Early steps in processing of yeast glycoproteins
    • Esmon, B., Esmon, P. C. & Schekman, R. (1984) Early steps in processing of yeast glycoproteins, J. Biol. Chem. 259, 10322-10327.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10322-10327
    • Esmon, B.1    Esmon, P.C.2    Schekman, R.3
  • 52
    • 2642702031 scopus 로고
    • Ultrastructural aspects of cellulase biosynthesis in Trichoderma reesei
    • (Kubicek, C. P., Eveleigh, D. E., Esterbauer, H., Steiner, W. & Kubicek-Pranz, E. M., eds) The Royal Society of Chemistry, Cambridge
    • Ghosh, B. K., Ganguly, T. & Ghosh, A. (1990) Ultrastructural aspects of cellulase biosynthesis in Trichoderma reesei, in Trichoderma reesei cellulases: biochemistry, genetics, physiology and application (Kubicek, C. P., Eveleigh, D. E., Esterbauer, H., Steiner, W. & Kubicek-Pranz, E. M., eds) pp. 115-138, The Royal Society of Chemistry, Cambridge.
    • (1990) Trichoderma Reesei Cellulases: Biochemistry, Genetics, Physiology and Application , pp. 115-138
    • Ghosh, B.K.1    Ganguly, T.2    Ghosh, A.3
  • 53
    • 0026788359 scopus 로고
    • Oligosaccharide structures of the major exoglucanase secreted by Saccharomyces cerevisiae
    • Hernández, L. M., Olivero, I., Alvarado, E. & Larriba, G. (1992) Oligosaccharide structures of the major exoglucanase secreted by Saccharomyces cerevisiae, Biochemistry 31, 9823-9831.
    • (1992) Biochemistry , vol.31 , pp. 9823-9831
    • Hernández, L.M.1    Olivero, I.2    Alvarado, E.3    Larriba, G.4
  • 54
    • 0023899375 scopus 로고
    • Control of glycoprotein synthesis. Purification and characterization of rabbit liver UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I
    • Nishikawa, Y., Pegg, W., Paulsen, H. & Schachter, H. (1988) Control of glycoprotein synthesis. Purification and characterization of rabbit liver UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I, J. Biol. Chem. 263, 8270-8281.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8270-8281
    • Nishikawa, Y.1    Pegg, W.2    Paulsen, H.3    Schachter, H.4
  • 55
    • 0030934154 scopus 로고    scopus 로고
    • NMR evidence for a novel asparagine-linked oligosaccharide on cellobiohydrolase I from Trichoderma reesei RUTC 30
    • in the press
    • De Bruyn, A., Maras, M., Schraml, J., Herdewijn, P. & Contreras, R. (1997) NMR evidence for a novel asparagine-linked oligosaccharide on cellobiohydrolase I from Trichoderma reesei RUTC 30, FEBS Lett. 405, in the press.
    • (1997) FEBS Lett. , vol.405
    • De Bruyn, A.1    Maras, M.2    Schraml, J.3    Herdewijn, P.4    Contreras, R.5


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