메뉴 건너뛰기




Volumn , Issue , 2010, Pages 127-144

Applications of mass spectrometry to analyze structure and bioactivity of chitooligosaccharides

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84958666604     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/EBK1439816035     Document Type: Chapter
Times cited : (3)

References (95)
  • 1
    • 0029619222 scopus 로고
    • A novel method for chemo-enzymic synthesis of elicitoractive chitosan oligomers and partially N-deacetylated chitin oligomers using N-acylated chitotrioses as substrates in a lysozyme-catalyzed transglycosylation reaction system
    • Akiyama, K., K. Kawazu, and A. Kobayashi. 1995. A novel method for chemo-enzymic synthesis of elicitoractive chitosan oligomers and partially N-deacetylated chitin oligomers using N-acylated chitotrioses as substrates in a lysozyme-catalyzed transglycosylation reaction system. Carbohydr. Res. 279: 151-160.
    • (1995) Carbohydr. Res , vol.279 , pp. 151-160
    • Akiyama, K.1    Kawazu, K.2    Kobayashi, A.3
  • 2
    • 0036060518 scopus 로고    scopus 로고
    • Sequence analysis of chito-oligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry
    • Bahrke, S, J. M. Einarsson, J. Gislason, S. Letzel, J. Peter-Katalinić, and M. G. Peter. 2002. Sequence analysis of chito-oligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry. Biomacromolecules 3: 696-704.
    • (2002) Biomacromolecules , vol.3 , pp. 696-704
    • Bahrke, S.1    Einarsson, J.M.2    Gislason, J.3    Letzel, S.4    Peter-Katalini, J.5    Ćpeter, M.G.6
  • 3
    • 33845573388 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of stable isotope labelled UDP-N-[2H]-acetyl-glucosamine and [2H]-acetyl-chito-oligosaccharides
    • Becker, H. F., A. Thellend, A. Piffeteau, and A. Vidal-Cros. 2006. Chemoenzymatic synthesis of stable isotope labelled UDP-N-[2H]-acetyl-glucosamine and [2H]-acetyl-chito-oligosaccharides. Glycoconj. J. 23: 687-692.
    • (2006) Glycoconj. J , vol.23 , pp. 687-692
    • Becker, H.F.1    Thellend, A.2    Piffeteau, A.3    Vidal-Cros, A.4
  • 4
    • 9744227158 scopus 로고    scopus 로고
    • Differential recognition of animal type β-4-galactosylated and α-3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum
    • Boer, H., N. Munck, J. Natunen, G. et al. 2004. Differential recognition of animal type β-4-galactosylated and α-3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum. Glycobiology 14: 1303-1313.
    • (2004) Glycobiology , vol.14 , pp. 1303-1313
    • Boer, H.1    Munck, N.2    Natunen, J.3
  • 5
    • 84989051538 scopus 로고
    • Characterization of glucosamine and N-acetylglucosamine oligomers by fast atom bombardment mass spectrometry
    • Bosso, C. and A. Domard. 1992. Characterization of glucosamine and N-acetylglucosamine oligomers by fast atom bombardment mass spectrometry. Org. Mass Spectrom. 27: 799-806.
    • (1992) Org. Mass Spectrom , vol.27 , pp. 799-806
    • Bosso, C.1    Domard, A.2
  • 6
    • 0002261005 scopus 로고
    • The behaviour of chitin towards anhydrous hydrogen fluoride. Preparation of β-(1→4)-linked 2-acetamido-2-deoxy-d-glucopyranosyl oligosaccharides
    • Bosso, C., J. Defaye, A. Domard, A. Gadelle, and C. Pedersen. 1986. The behaviour of chitin towards anhydrous hydrogen fluoride. Preparation of β-(1→4)-linked 2-acetamido-2-deoxy-d-glucopyranosyl oligosaccharides. Carbohydr. Res. 156: 57-68.
    • (1986) Carbohydr. Res , vol.156 , pp. 57-68
    • Bosso, C.1    Defaye, J.2    Domard, A.3    Gadelle, A.4    Pedersen, C.5
  • 7
    • 0242291106 scopus 로고    scopus 로고
    • Applications of electronion dissociation reactions for analysis of polycationic chitooligosaccharides in Fourier transform mass spectrometry
    • Budnik, B. A., K. F. Haselmann, Y. N. Elkin, V. I. Gorbach, and R. A. Zubarev. 2003. Applications of electronion dissociation reactions for analysis of polycationic chitooligosaccharides in Fourier transform mass spectrometry. Anal. Chem. 75: 5994-6001.
    • (2003) Anal. Chem , vol.75 , pp. 5994-6001
    • Budnik, B.A.1    Haselmann, K.F.2    Elkin, Y.N.3    Gorbach, V.I.4    Zubarev, R.A.5
  • 8
    • 33845449090 scopus 로고    scopus 로고
    • Global methods for protein glycosylation analysis by mass spectrometry
    • Budnik, B. A., R. S. Lee, and J. A. J. Steen. 2006. Global methods for protein glycosylation analysis by mass spectrometry. Biochim. Biophys. Acta 1764: 1870-1880.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1870-1880
    • Budnik, B.A.1    Lee, R.S.2    Steen, J.A.J.3
  • 9
    • 23644434818 scopus 로고    scopus 로고
    • Preparation of chitooligosaccharides with degree of polymerization higher than 6 by acid or enzymatic degradation of chitosan
    • Cabrera, J. C. and P. van Cutsem. 2005. Preparation of chitooligosaccharides with degree of polymerization higher than 6 by acid or enzymatic degradation of chitosan. Biochem. Eng. J. 25: 165-172.
    • (2005) Biochem. Eng. J , vol.25 , pp. 165-172
    • Cabrera, J.C.1    Van Cutsem, P.2
  • 10
    • 33645877068 scopus 로고    scopus 로고
    • Size, acetylation and concentration of chitooligosaccharide elicitors determine the switch from defence involving PAL activation to cell death and water peroxide production in Arabidopsis cell suspensions
    • Cabrera, J. C., J. Messiaen, P. Cambier, and P. van Cutsem. 2006. Size, acetylation and concentration of chitooligosaccharide elicitors determine the switch from defence involving PAL activation to cell death and water peroxide production in Arabidopsis cell suspensions. Physiol. Plantarum 127: 44-56.
    • (2006) Physiol. Plantarum , vol.127 , pp. 44-56
    • Cabrera, J.C.1    Messiaen, J.2    Cambier, P.3    Van Cutsem, P.4
  • 11
    • 0032774471 scopus 로고    scopus 로고
    • Fragmentation reactions in the mass spectrometry analysis of neutral oligosaccharides
    • Cancilla, M. T., A. W. Wong, L. R. Voss, and C. B. Lebrilla. 1999. Fragmentation reactions in the mass spectrometry analysis of neutral oligosaccharides. Anal. Chem. 71: 3206-3218.
    • (1999) Anal. Chem , vol.71 , pp. 3206-3218
    • Cancilla, M.T.1    Wong, A.W.2    Voss, L.R.3    Lebrilla, C.B.4
  • 12
    • 33746283059 scopus 로고    scopus 로고
    • Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-offlight tandem mass spectrometry of a noncovalent enzyme-ligand complex
    • Cederkvist, F., A. D. Zamfir, S. Bahrke, V. G. H. Eijsink, M. Sørlie, J. Peter-Katalinic´, and M. G. Peter. 2006. Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-offlight tandem mass spectrometry of a noncovalent enzyme-ligand complex. Angew. Chem. Int. Ed. 45: 2429-2434.
    • (2006) Angew. Chem. Int. Ed , vol.45 , pp. 2429-2434
    • Cederkvist, F.1    Zamfir, A.D.2    Bahrke, S.3    Eijsink, V.G.H.4    Sørlie, M.5    Peter-Katalinic´, J.6    Peter, M.G.7
  • 14
    • 0034127012 scopus 로고    scopus 로고
    • A probe for the versatile analysis and characterization of N-linked oligosaccharides
    • Charlwood, J., H. Birrell, A. Gribble, V. Burdes, D. Tolson, and P. Camilleri. 2000. A probe for the versatile analysis and characterization of N-linked oligosaccharides. Anal. Chem. 72: 1453-1461.
    • (2000) Anal. Chem , vol.72 , pp. 1453-1461
    • Charlwood, J.1    Birrell, H.2    Gribble, A.3    Burdes, V.4    Tolson, D.5    Camilleri, P.6
  • 15
    • 17144419243 scopus 로고    scopus 로고
    • A chitosanase from Paecilomyces lilacinus with binding affinity for specific chito-oligosaccharides
    • Chen, Y. Y., C. Y. Cheng, T. L. Haung, and Y. K. Li. 2005. A chitosanase from Paecilomyces lilacinus with binding affinity for specific chito-oligosaccharides. Biotechnol. Appl. Biochem. 41: 145-150.
    • (2005) Biotechnol. Appl. Biochem , vol.41 , pp. 145-150
    • Chen, Y.Y.1    Cheng, C.Y.2    Haung, T.L.3    Li, Y.K.4
  • 16
    • 34247886097 scopus 로고    scopus 로고
    • Gene cloning and characterization of a novel recombinant antifungal chitinase from papaya (Carica papaya)
    • Chen, Y. T., L. H. Hsu, I. P. Huang, T. C. Tsai, G. C. Lee, and J. F. Shaw. 2007. Gene cloning and characterization of a novel recombinant antifungal chitinase from papaya (Carica papaya). J. Agric. Food Chem. 55: 714-722.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 714-722
    • Chen, Y.T.1    Hsu, L.H.2    Huang, I.P.3    Tsai, T.C.4    Lee, G.C.5    Shaw, J.F.6
  • 17
    • 33645642460 scopus 로고    scopus 로고
    • Exploration of glycosyl hydrolase family 75, a chitosanase from Aspergillus fumigatus
    • Cheng, C. Y., C. H. Chang, Y. J. Wu, and Y. K. Li. 2006. Exploration of glycosyl hydrolase family 75, a chitosanase from Aspergillus fumigatus. J. Biol. Chem. 281: 3137-3144.
    • (2006) J. Biol. Chem , vol.281 , pp. 3137-3144
    • Cheng, C.Y.1    Chang, C.H.2    Wu, Y.J.3    Li, Y.K.4
  • 18
    • 0017577860 scopus 로고
    • Structure determination of N-acetyl amino sugar derivatives and disaccharides by gas chromatography and mass spectroscopy. Anal
    • Coduti, P. L. and C. A. Bush. 1977. Structure determination of N-acetyl amino sugar derivatives and disaccharides by gas chromatography and mass spectroscopy. Anal. Biochem. 78: 21-38.
    • (1977) Biochem , vol.78 , pp. 21-38
    • Coduti, P.L.1    Bush, C.A.2
  • 19
    • 0033851083 scopus 로고    scopus 로고
    • A fluorescence-quenched chitopentaose for the study of endochitinases and chitobiosidases
    • Cottaz, S., B. Brasme, and H. Driguez. 2000. A fluorescence-quenched chitopentaose for the study of endochitinases and chitobiosidases. Eur. J. Biochem. 267: 5593-5600.
    • (2000) Eur. J. Biochem , vol.267 , pp. 5593-5600
    • Cottaz, S.1    Brasme, B.2    Driguez, H.3
  • 22
    • 33748995918 scopus 로고    scopus 로고
    • Mass spectrometric real-time monitoring of enzymatic glycosidic hydrolysis, enzymatic inhibition and enzyme complexes
    • Dennhart, N. and T. Letzel. 2006. Mass spectrometric real-time monitoring of enzymatic glycosidic hydrolysis, enzymatic inhibition and enzyme complexes. Anal. Bioanal. Chem. 386: 689-698.
    • (2006) Anal. Bioanal. Chem , vol.386 , pp. 689-698
    • Dennhart, N.1    Letzel, T.2
  • 23
    • 41549102790 scopus 로고    scopus 로고
    • Oligosaccharide hydrolysis by chitosanase enzymes monitored by real-time electrospray ionization-mass spectrometry
    • Dennhart, N., T. Fukamizo, R. Brzezinski, M.-E. Lacombe-Harvey, and T. Letzel. 2008. Oligosaccharide hydrolysis by chitosanase enzymes monitored by real-time electrospray ionization-mass spectrometry. J. Biotechnol. 134: 253-260.
    • (2008) J. Biotechnol , vol.134 , pp. 253-260
    • Dennhart, N.1    Fukamizo, T.2    Brzezinski, R.3    Lacombe-Harvey, M.-E.4    Letzel, T.5
  • 26
    • 79951510738 scopus 로고    scopus 로고
    • Pharmaceutical composition comprising chitooligomers
    • WO 03/026677 Primex Ehf., Iceland
    • Einarsson, J. M., J. Gislason, M. G. Peter, and S. Bahrke. 2003. Pharmaceutical composition comprising chitooligomers. PCT Int. Appl. WO 03/026677 Primex Ehf., Iceland, 30 pp.
    • (2003) PCT Int. Appl , pp. 30
    • Einarsson, J.M.1    Gislason, J.2    Peter, M.G.3    Bahrke, S.4
  • 27
    • 33947169226 scopus 로고    scopus 로고
    • Introduction to ion trap mass spectrometry: Application to the structural characterization of plant oligosaccharides
    • Fernandez, L. E. M. 2007. Introduction to ion trap mass spectrometry: Application to the structural characterization of plant oligosaccharides. Carbohydr. Polym. 68: 797-807.
    • (2007) Carbohydr. Polym , vol.68 , pp. 797-807
    • Fernandez, L.E.M.1
  • 29
    • 0343071628 scopus 로고
    • Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry
    • Ganem, B. 1991. Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry. J. Am. Chem. Soc. 119: 7818-7819.
    • (1991) J. Am. Chem. Soc , vol.119 , pp. 7818-7819
    • Ganem, B.1
  • 30
    • 0038137349 scopus 로고    scopus 로고
    • Solution-and bound-state conformational study of N, N′N″-triacetyl chitotriose and other analogous potential inhibitors of hevamine: Application of trNOESY and STD NMR spectroscopy
    • Germer, A., C. Mügge, M. G. Peter, A. Rottmann, and E. Kleinpeter. 2003. Solution-and bound-state conformational study of N, N′N″-triacetyl chitotriose and other analogous potential inhibitors of hevamine: Application of trNOESY and STD NMR spectroscopy. Chem. Eur. J. 9: 1964-1973.
    • (2003) Chem. Eur. J , vol.9 , pp. 1964-1973
    • Germer, A.1    Mügge, C.2    Peter, M.G.3    Rottmann, A.4    Kleinpeter, E.5
  • 31
    • 34547812494 scopus 로고    scopus 로고
    • Quantitative sequencing of complex mixtures of heterochitooligosaccharides by vMALDI-linear ion trap mass spectrometry
    • Haebel, S., S. Bahrke, and M. G. Peter. 2007. Quantitative sequencing of complex mixtures of heterochitooligosaccharides by vMALDI-linear ion trap mass spectrometry. Anal. Chem. 79: 5557-5566.
    • (2007) Anal. Chem , vol.79 , pp. 5557-5566
    • Haebel, S.1    Bahrke, S.2    Peter, M.G.3
  • 32
    • 0033597847 scopus 로고    scopus 로고
    • Structural studies of N-glycans of filarial parasites. Conservation of phosphorylcholine-substituted glycans among species and discovery of novel chito-oligomers
    • Haslam, S. M., K. M. Houston, W. Harnett, A. J. Reason, H. R. Morris, and A. Dell. 1999. Structural studies of N-glycans of filarial parasites. Conservation of phosphorylcholine-substituted glycans among species and discovery of novel chito-oligomers. J. Biol. Chem. 274: 20953-20960.
    • (1999) J. Biol. Chem , vol.274 , pp. 20953-20960
    • Haslam, S.M.1    Houston, K.M.2    Harnett, W.3    Reason, A.J.4    Morris, H.R.5    Dell, A.6
  • 33
    • 0033590021 scopus 로고    scopus 로고
    • Evidence for enzymatic activity in the absence of solvent in gasphase complexes of lysozyme and oligosaccharides
    • He, F., J. Ramirez, and C. B. Lebrilla. 1999. Evidence for enzymatic activity in the absence of solvent in gasphase complexes of lysozyme and oligosaccharides. Int. J. Mass Spectrom. 193: 103-114.
    • (1999) Int. J. Mass Spectrom , vol.193 , pp. 103-114
    • He, F.1    Ramirez, J.2    Lebrilla, C.B.3
  • 34
    • 0042330067 scopus 로고    scopus 로고
    • Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: An investigation using steady-state kinetic analysis and MS
    • Hekmat, O., K. Tokuyasu, and S. G. Withers. 2003. Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: An investigation using steady-state kinetic analysis and MS. Biochem. J. 374: 369-380.
    • (2003) Biochem. J , vol.374 , pp. 369-380
    • Hekmat, O.1    Tokuyasu, K.2    Withers, S.G.3
  • 36
    • 33644935876 scopus 로고    scopus 로고
    • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
    • Horn, S. J., A. Sørbotten, B. Synstad et al. 2006. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 273: 491-503.
    • (2006) FEBS J , vol.273 , pp. 491-503
    • Horn, S.J.1    Sørbotten, A.2    Synstad, B.3
  • 37
    • 79951512117 scopus 로고    scopus 로고
    • PhD thesis, University of Potsdam, Potsdam, Germany
    • Issaree, A. 2008. Synthesis of hetero-chitooligosaccharides. PhD thesis, University of Potsdam, Potsdam, Germany. URL: http://opus.kobv.de/ubp/volltexte/2008/1706/.
    • (2008) Synthesis of Hetero-Chitooligosaccharides
    • Issaree, A.1
  • 39
    • 65249134395 scopus 로고    scopus 로고
    • Mass spectrometric analysis using ruthenium (II)-labelling for identification of glycosyl hydrolase product. Biosci. Biotechnol
    • Ito, A., T. A. Okamura, K. Uegaki et al. 2009. Mass spectrometric analysis using ruthenium (II)-labelling for identification of glycosyl hydrolase product. Biosci. Biotechnol. Biochem. 73: 428-430.
    • (2009) Biochem , vol.73 , pp. 428-430
    • Ito, A.1    Okamura, T.A.2    Uegaki, K.3
  • 40
    • 85055237786 scopus 로고
    • Action pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan
    • C. J. Brine, P. A. Sandford, and J. P. Zikakis, London, U.K.: Elsevier
    • Izume, M., S. Nagae, H. Kawagishi, M. Mitsutomi, and A. Ohtakara. 1992. Action pattern of Bacillus sp. no. 7-M chitosanase on partially N-acetylated chitosan. In Advances in Chitin and Chitosan, eds., C. J. Brine, P. A. Sandford, and J. P. Zikakis, pp. 334-343. London, U.K.: Elsevier.
    • (1992) Advances in Chitin and Chitosan , pp. 334-343
    • Izume, M.1    Nagae, S.2    Kawagishi, H.3    Mitsutomi, M.4    Ohtakara, A.5
  • 41
    • 0028787218 scopus 로고
    • Mass spectrometric analysis of chitin oligosaccharides produced by Rhizobium NodC protein in Escherichia coli
    • Kamst, E., K. M. G. M. van der Drift, J. E. Thomas-Oates, B. J. J. Lugtenberg, and H. P. Spaink. 1995. Mass spectrometric analysis of chitin oligosaccharides produced by Rhizobium NodC protein in Escherichia coli. J. Bacteriol. 177: 6282-6285.
    • (1995) J. Bacteriol , vol.177 , pp. 6282-6285
    • Kamst, E.1    Van Der Drift, K.M.G.M.2    Thomas-Oates, J.E.3    Lugtenberg, B.J.J.4    Spaink, H.P.5
  • 42
    • 0035700089 scopus 로고    scopus 로고
    • Purification and properties of extracellular chitinases from the parasitic fungus Isaria japonica
    • Kawachi, I., T. Fujieda, M. Ujita, et al. 2001. Purification and properties of extracellular chitinases from the parasitic fungus Isaria japonica. J. Biosci. Bioeng. 92: 544-549.
    • (2001) J. Biosci. Bioeng , vol.92 , pp. 544-549
    • Kawachi, I.1    Fujieda, T.2    Ujita, M.3
  • 43
    • 0037402769 scopus 로고    scopus 로고
    • Microanalysis of N-linked oligosaccharides in a glycoprotein by capillary liquid chromatography/mass spectrometry and liquid chromatography/tandem mass spectrometry
    • Kawasaki, N., S. Itoh, M. Ohta, and T. Hayakawa. 2003. Microanalysis of N-linked oligosaccharides in a glycoprotein by capillary liquid chromatography/mass spectrometry and liquid chromatography/tandem mass spectrometry. Anal. Biochem. 316: 15-22.
    • (2003) Anal. Biochem , vol.316 , pp. 15-22
    • Kawasaki, N.1    Itoh, S.2    Ohta, M.3    Hayakawa, T.4
  • 44
    • 0033166283 scopus 로고    scopus 로고
    • Mass spectrometric profiling of glucosamine, glucosamine polymers and their catecholamine adducts: Model reactions and cuticular hydrolysates of Toxorhynchites amboinensis (Culicidae) pupae
    • Kerwin, J. L., D. L. Whitney, and A. Sheikh. 1999. Mass spectrometric profiling of glucosamine, glucosamine polymers and their catecholamine adducts: Model reactions and cuticular hydrolysates of Toxorhynchites amboinensis (Culicidae) pupae. Insect Biochem. Mol. Biol. 29: 599-607.
    • (1999) Insect Biochem. Mol. Biol , vol.29 , pp. 599-607
    • Kerwin, J.L.1    Whitney, D.L.2    Sheikh, A.3
  • 45
    • 28544437497 scopus 로고    scopus 로고
    • Enzymatic production and biological activities of chitosan oligosaccharides (COS): A review
    • Kim, S. K. and N. Rajapakse. 2005. Enzymatic production and biological activities of chitosan oligosaccharides (COS): A review. Carbohydr. Polym. 62: 357-368.
    • (2005) Carbohydr. Polym , vol.62 , pp. 357-368
    • Kim, S.K.1    Rajapakse, N.2
  • 46
    • 0037411897 scopus 로고    scopus 로고
    • Chitosanolysis by a pectinase isozyme of Aspergillus niger: A non-specific activity
    • Kittur, F. S., A. B. V. Kumar, L. R. Gowda, and R. N. Tharanathan. 2003. Chitosanolysis by a pectinase isozyme of Aspergillus niger: A non-specific activity. Carbohydr. Polym. 53: 191-196.
    • (2003) Carbohydr. Polym , vol.53 , pp. 191-196
    • Kittur, F.S.1    Kumar, A.B.V.2    Gowda, L.R.3    Tharanathan, R.N.4
  • 47
    • 15944398651 scopus 로고    scopus 로고
    • Chitooligosaccharides: Preparation with the aid of pectinase isozyme from Aspergillus niger and their antibacterial activity
    • Kittur, F. S., A. B. V. Kumar, M. C. Varadaraj, and R. N. Tharanathan. 2005. Chitooligosaccharides: Preparation with the aid of pectinase isozyme from Aspergillus niger and their antibacterial activity. Carbohydr. Res. 340: 1239-1245.
    • (2005) Carbohydr. Res , vol.340 , pp. 1239-1245
    • Kittur, F.S.1    Kumar, A.B.V.2    Varadaraj, M.C.3    Tharanathan, R.N.4
  • 48
    • 0036982053 scopus 로고    scopus 로고
    • Chitosan oligosaccharides, DP 2-8, have prebiotic effect on the Bifidobacterium bifidum and Lactobacillus sp
    • Lee, H.-W., Y.-S. Park, J.-S. Jung, and W.-S. Shin. 2003. Chitosan oligosaccharides, DP 2-8, have prebiotic effect on the Bifidobacterium bifidum and Lactobacillus sp. Anaerobe 8: 319-324.
    • (2003) Anaerobe , vol.8 , pp. 319-324
    • Lee, H.-W.1    Park, Y.-S.2    Jung, J.-S.3    Shin, W.-S.4
  • 49
    • 0005607709 scopus 로고    scopus 로고
    • Libraries of chitooligosaccharides of mixed acetylation patterns and their interactions with chitinases
    • Letzel, M. C., B. Synstad, V. G. H. Eijsink, J. Peter-Katalinić, and M. G. Peter. 2000. Libraries of chitooligosaccharides of mixed acetylation patterns and their interactions with chitinases. Adv. Chitin Sci. 4: 545-552.
    • (2000) Adv. Chitin Sci , vol.4 , pp. 545-552
    • Letzel, M.C.1    Synstad, B.2    Eijsink, V.G.H.3    Peter-Katalini, J.4    Ćpeter, M.G.5
  • 50
    • 12444281793 scopus 로고    scopus 로고
    • Preparation and characterization of low molecular weight chitosan and chito-oligomers by a commercial enzyme
    • Li, J., Y. Du, J. Yang, T. Feng, A. Li, and P. Chen. 2005. Preparation and characterization of low molecular weight chitosan and chito-oligomers by a commercial enzyme. Polym. Degrad. Stab. 87: 441-448.
    • (2005) Polym. Degrad. Stab , vol.87 , pp. 441-448
    • Li, J.1    Du, Y.2    Yang, J.3    Feng, T.4    Li, A.5    Chen, P.6
  • 51
    • 33749476846 scopus 로고    scopus 로고
    • Low molecular weight water-soluble chitosans: Preparation with the aid of cellulase, characterization, and solubility
    • Li, J., Y. M. Du, and H. B. Liang. 2006a. Low molecular weight water-soluble chitosans: Preparation with the aid of cellulase, characterization, and solubility. J. Appl. Polym. Sci. 102: 1098-1105.
    • (2006) J. Appl. Polym. Sci , vol.102 , pp. 1098-1105
    • Li, J.1    Du, Y.M.2    Liang, H.B.3
  • 52
    • 33751235229 scopus 로고    scopus 로고
    • Effect of immobilized neutral protease on the preparation and physicochemical properties of low molecular weight chitosan and chito-oligomers
    • Li, J., Y. M. Du, H. B. Liang, P. J. Yao, and Y. A. Wei. 2006b. Effect of immobilized neutral protease on the preparation and physicochemical properties of low molecular weight chitosan and chito-oligomers. J. Appl. Polym. Sci. 102: 4185-4193.
    • (2006) J. Appl. Polym. Sci , vol.102 , pp. 4185-4193
    • Li, J.1    Du, Y.M.2    Liang, H.B.3    Yao, P.J.4    Wei, Y.A.5
  • 53
    • 36249003867 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio cholerae: Characterization of a unique chitin oligosaccharide deacetylase
    • Li, X., L.-X. Wang, X. Wang, and S. Roseman. 2007. The chitin catabolic cascade in the marine bacterium Vibrio cholerae: Characterization of a unique chitin oligosaccharide deacetylase. Glycobiology 17: 1377-1387.
    • (2007) Glycobiology , vol.17 , pp. 1377-1387
    • Li, X.1    Wang, L.-X.2    Wang, X.3    Roseman, S.4
  • 54
    • 55849122624 scopus 로고    scopus 로고
    • Effect of sonolysis on kinetics and physicochemical properties of treated chitosan
    • Li, J., J. Cai, and L. H. Fan. 2008. Effect of sonolysis on kinetics and physicochemical properties of treated chitosan. J. Appl. Polym. Sci. 109: 2417-2425.
    • (2008) J. Appl. Polym. Sci , vol.109 , pp. 2417-2425
    • Li, J.1    Cai, J.2    Fan, L.H.3
  • 55
    • 0037015411 scopus 로고    scopus 로고
    • Preparation of chitosan oligomers by immobilized papain
    • Lin, H., H. Wang, C. Xue, and M. Ye. 2002. Preparation of chitosan oligomers by immobilized papain. Enzyme Microb. Technol. 31: 588-592.
    • (2002) Enzyme Microb. Technol , vol.31 , pp. 588-592
    • Lin, H.1    Wang, H.2    Xue, C.3    Ye, M.4
  • 56
    • 0028999965 scopus 로고
    • Mass-spectrometric analysis of N-acetylchito-oligosaccharides prepared through enzymic hydrolysis of chitosan
    • Lopatin, S. A., M. M. Ilyin, V. N. Pustobaev, Z. A. Bezchetnikova, V. P. Varlamov, and V. A. Davankov. 1995. Mass-spectrometric analysis of N-acetylchito-oligosaccharides prepared through enzymic hydrolysis of chitosan. Anal. Biochem. 227: 285-288.
    • (1995) Anal. Biochem , vol.227 , pp. 285-288
    • Lopatin, S.A.1    Ilyin, M.M.2    Pustobaev, V.N.3    Bezchetnikova, Z.A.4    Varlamov, V.P.5    Davankov, V.A.6
  • 57
    • 33846254015 scopus 로고    scopus 로고
    • Chitinase-catalyzed copolymerization to a chitin derivative having glucosamine unit in controlled proportion
    • Makino, A., M. Ohmae, and S. Kobayashi. 2006a. Chitinase-catalyzed copolymerization to a chitin derivative having glucosamine unit in controlled proportion. Polymer J. 38: 1182-1188.
    • (2006) Polymer J , vol.38 , pp. 1182-1188
    • Makino, A.1    Ohmae, M.2    Kobayashi, S.3
  • 58
    • 33645532259 scopus 로고    scopus 로고
    • Chitinase-catalyzed synthesis of alternatingly N-deacetylated chitin: A chitin-chitosan hybrid polysaccharide
    • Makino, A., K. Kurosaki, M. Ohmae, and S. Kobayashi. 2006b. Chitinase-catalyzed synthesis of alternatingly N-deacetylated chitin: A chitin-chitosan hybrid polysaccharide. Biomacromolecules 7: 950-957.
    • (2006) Biomacromolecules , vol.7 , pp. 950-957
    • Makino, A.1    Kurosaki, K.2    Ohmae, M.3    Kobayashi, S.4
  • 59
    • 0001039236 scopus 로고    scopus 로고
    • Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan
    • R. A. A. Muzzarelli, Grottamare, Italy: Atec
    • Mitsutomi, M., M. Ueda, M. Arai, A. Ando, and T. Watanabe. 1996. Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan. In: Chitin Enzymology, Vol. 2, ed. R. A. A. Muzzarelli, pp. 272-284. Grottamare, Italy: Atec.
    • (1996) Chitin Enzymology , vol.2 , pp. 272-284
    • Mitsutomi, M.1    Ueda, M.2    Arai, M.3    Ando, A.4    Watanabe, T.5
  • 61
    • 85055216003 scopus 로고    scopus 로고
    • Characteristics of a 49-kDa chitinase from Streptomyces griseus Hut 6037
    • Mitsutomi, M., T. Tanabe, R. Kanai, and T. Watanabe. 1998. Characteristics of a 49-kDa chitinase from Streptomyces griseus Hut 6037. Advan. Chitin Sci. 3: 221-226.
    • (1998) Advan. Chitin Sci , vol.3 , pp. 221-226
    • Mitsutomi, M.1    Tanabe, T.2    Kanai, R.3    Watanabe, T.4
  • 62
    • 0029175060 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry: Improved matrix for oligosaccharides
    • Mohr, M. D., K. O. Boernsen, and H. M. Widmer. 1995. Matrix-assisted laser desorption/ionization mass spectrometry: Improved matrix for oligosaccharides. Rapid Commun. Mass Spectrom. 9: 809-814.
    • (1995) Rapid Commun. Mass Spectrom , vol.9 , pp. 809-814
    • Mohr, M.D.1    Boernsen, K.O.2    Widmer, H.M.3
  • 63
    • 85055225707 scopus 로고
    • Preparation of chitooligosaccharidealditols by hydrogenation with ruthenium catalyst
    • C. J. Brine, P. A. Sandford, and J. P. Zikakis, London, U.K.: Elsevier
    • Nagae, S., M. Izume, S. Nishimura, H. Kawagishi, and A Ohtakara. 1992. Preparation of chitooligosaccharidealditols by hydrogenation with ruthenium catalyst. In Advances in Chitin and Chitosan, eds. C. J. Brine, P. A. Sandford, and J. P. Zikakis, pp. 378-384. London, U.K.: Elsevier.
    • (1992) Advances in Chitin and Chitosan , pp. 378-384
    • Nagae, S.1    Izume, M.2    Nishimura, S.3    Kawagishi, H.4    Ohtakara, A.5
  • 64
    • 0034743944 scopus 로고    scopus 로고
    • Human α3-fucosyltransferases convert chitin oligosaccharides to products containing a GlcNAcß1-4(Fucα1-3)GlcNAcß1-4R determinant at the nonreducing terminus
    • Natunen, J., O. Aitio, J. Helin et al. 2001. Human α3-fucosyltransferases convert chitin oligosaccharides to products containing a GlcNAcß1-4(Fucα1-3)GlcNAcß1-4R determinant at the nonreducing terminus. Glycobiology 11: 209-216.
    • (2001) Glycobiology , vol.11 , pp. 209-216
    • Natunen, J.1    Aitio, O.2    Helin, J.3
  • 65
    • 0000758635 scopus 로고    scopus 로고
    • Cationic derivatization of oligosaccharides with Girard’s T reagent for improved performance in matrix-assisted laser desorption ionization and electrospray mass spectrometry
    • Naven, T. J. P. and D. J. Harvey. 1996. Cationic derivatization of oligosaccharides with Girard’s T reagent for improved performance in matrix-assisted laser desorption ionization and electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 10: 829-834.
    • (1996) Rapid Commun. Mass Spectrom , vol.10 , pp. 829-834
    • Naven, T.J.P.1    Harvey, D.J.2
  • 66
    • 46649119277 scopus 로고    scopus 로고
    • Chitin oligosaccharides inhibit oxidative stress in live cells
    • Ngo, D. N., M. M. Kim, and S. K. Kim. 2008. Chitin oligosaccharides inhibit oxidative stress in live cells. Carbohydr. Polym. 74: 228-234.
    • (2008) Carbohydr. Polym , vol.74 , pp. 228-234
    • Ngo, D.N.1    Kim, M.M.2    Kim, S.K.3
  • 67
    • 0030853595 scopus 로고    scopus 로고
    • Minimizing cationization effects in the analysis of complex mixtures of oligosaccharides
    • North, S., G. Okafo, H. Birelli, N. Haskins, and P. Camilleri. 1997. Minimizing cationization effects in the analysis of complex mixtures of oligosaccharides. Rapid Commun. Mass Spectrom. 11: 1635-1642.
    • (1997) Rapid Commun. Mass Spectrom , vol.11 , pp. 1635-1642
    • North, S.1    Okafo, G.2    Birelli, H.3    Haskins, N.4    Camilleri, P.5
  • 68
    • 0031573567 scopus 로고    scopus 로고
    • High-performance liquid chromatographic analysis of complex N-linked glycans derivatized with 2-aminoacridone
    • Okafo, G., J. Langridge, S. North et al. 1997. High-performance liquid chromatographic analysis of complex N-linked glycans derivatized with 2-aminoacridone. Anal. Chem. 69: 4985-4993.
    • (1997) Anal. Chem , vol.69 , pp. 4985-4993
    • Okafo, G.1    Langridge, J.2    North, S.3
  • 69
    • 49249128067 scopus 로고    scopus 로고
    • Growth of phytopathogenic fungi in the presence of partially acetylated chitooligosaccharides
    • Oliveira, E. N., N. E. El Gueddari, B. M. Moerschbacher, M. G. Peter, and T. T. Franco. 2008. Growth of phytopathogenic fungi in the presence of partially acetylated chitooligosaccharides. Mycopathologia 166: 163-174.
    • (2008) Mycopathologia , vol.166 , pp. 163-174
    • Oliveira, E.N.1    El Gueddari, N.E.2    Moerschbacher, B.M.3    Peter, M.G.4    Franco, T.T.5
  • 70
    • 0344835732 scopus 로고    scopus 로고
    • Novel branched nod factor structure results from α-(1→3) fucosyl transferase activity: The major lipo-chitin oligosaccharides from Mesorhizobium loti strain NZP2213 bear an α-(1→3) fucosyl substituent on a nonterminal backbone residue
    • Olsthoorn, M. M. A., I. M. Lopez-Lara, B. O. Petersen et al. 1998. Novel branched nod factor structure results from α-(1→3) fucosyl transferase activity: The major lipo-chitin oligosaccharides from Mesorhizobium loti strain NZP2213 bear an α-(1→3) fucosyl substituent on a nonterminal backbone residue. Biochemistry 37: 9024-9032.
    • (1998) Biochemistry , vol.37 , pp. 9024-9032
    • Olsthoorn, M.M.A.1    Lopez-Lara, I.M.2    Petersen, B.O.3
  • 71
    • 33947580842 scopus 로고    scopus 로고
    • Inhibitory analysis of the effect of polycyclic aromatic hydrocarbons on the activity of chitinase by means of liquid chromatography-mass spectrometry of chitin oligosaccharides
    • Ooki, Y., M. Kumemura, M. Itoh, and T. Korenaga. 2007. Inhibitory analysis of the effect of polycyclic aromatic hydrocarbons on the activity of chitinase by means of liquid chromatography-mass spectrometry of chitin oligosaccharides. Anal. Bioanal. Chem. 387: 2641-2644.
    • (2007) Anal. Bioanal. Chem , vol.387 , pp. 2641-2644
    • Ooki, Y.1    Kumemura, M.2    Itoh, M.3    Korenaga, T.4
  • 73
    • 0842310465 scopus 로고    scopus 로고
    • Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay
    • Pi, N. and J. A. Leary. 2004. Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay. J. Am. Soc. Mass Spectrom. 15: 233-243.
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 233-243
    • Pi, N.1    Leary, J.A.2
  • 74
    • 33746858905 scopus 로고    scopus 로고
    • Oligosaccharide structures studied by hydrogen-deuterium exchange and MALDI-TOF mass spectrometry
    • Price, N. P. J. 2006. Oligosaccharide structures studied by hydrogen-deuterium exchange and MALDI-TOF mass spectrometry. Anal. Chem. 78: 5302-5308.
    • (2006) Anal. Chem , vol.78 , pp. 5302-5308
    • Price, N.P.J.1
  • 75
    • 0030759788 scopus 로고    scopus 로고
    • Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli
    • Samain, E., S. Drouillard, A. Heyraud, H. Driguez, and R. A. Geremia. 1997. Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli. Carbohydr. Res. 302: 35-42.
    • (1997) Carbohydr. Res , vol.302 , pp. 35-42
    • Samain, E.1    Drouillard, S.2    Heyraud, A.3    Driguez, H.4    Geremia, R.A.5
  • 76
    • 0028095458 scopus 로고
    • Capillary zone electrophoresis and micellar electrokinetic chromatography of 4-aminobenzonitrile carbohydrate derivatives
    • Schwaiger, H., P. J. Oefnel, C. Huber, E. Grill, and G. K. Bonn. 1994. Capillary zone electrophoresis and micellar electrokinetic chromatography of 4-aminobenzonitrile carbohydrate derivatives. Electrophoresis 15: 941-952.
    • (1994) Electrophoresis , vol.15 , pp. 941-952
    • Schwaiger, H.1    Oefnel, P.J.2    Huber, C.3    Grill, E.4    Bonn, G.K.5
  • 77
    • 0030725487 scopus 로고    scopus 로고
    • Investigation of copper-saccharide complexation reactions using potentiometry and electrospray mass spectrometry
    • Shabgholi, M., J. H. Callahan, B. J. Rappoli, and D. A. Rowley. 1997. Investigation of copper-saccharide complexation reactions using potentiometry and electrospray mass spectrometry. J. Mass Spectrom. 32: 1080-1093.
    • (1997) J. Mass Spectrom , vol.32 , pp. 1080-1093
    • Shabgholi, M.1    Callahan, J.H.2    Rappoli, B.J.3    Rowley, D.A.4
  • 78
    • 0028853934 scopus 로고
    • Glycosidase-catalyzed oligosaccharide synthesis: Preparation of the N-acetylchito-oligosaccharides penta-N-acetylchitopentaose and hexa-Nacetylchitohexaose using the β-N-acetylhexosaminidase of Aspergillus oryzae
    • Singh, S., R. Gallagher, P. J. Derrick, and D. H. G. Crout. 1995. Glycosidase-catalyzed oligosaccharide synthesis: Preparation of the N-acetylchito-oligosaccharides penta-N-acetylchitopentaose and hexa-Nacetylchitohexaose using the β-N-acetylhexosaminidase of Aspergillus oryzae. Tetrahedron: Asymm. 6: 2803-2810.
    • (1995) Tetrahedron: Asymm , vol.6 , pp. 2803-2810
    • Singh, S.1    Gallagher, R.2    Derrick, P.J.3    Crout, D.H.G.4
  • 79
    • 0030658110 scopus 로고    scopus 로고
    • Post-source decay analysis in matrix-assisted laser desorption/ionization mass spectrometry of biomolecules
    • Spengler, B. 1997. Post-source decay analysis in matrix-assisted laser desorption/ionization mass spectrometry of biomolecules. J. Mass Spectrom. 32: 1019-1036.
    • (1997) J. Mass Spectrom , vol.32 , pp. 1019-1036
    • Spengler, B.1
  • 80
    • 22144480668 scopus 로고    scopus 로고
    • Enzymatic properties of wildtype and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS
    • Suginta, W., A. Vongsuwan, C. Songsiriritthigul, J. Svasti, and H. Prinz. 2005. Enzymatic properties of wildtype and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS. FEBS J. 272: 3376-3386.
    • (2005) FEBS J , vol.272 , pp. 3376-3386
    • Suginta, W.1    Vongsuwan, A.2    Songsiriritthigul, C.3    Svasti, J.4    Prinz, H.5
  • 81
    • 0042127130 scopus 로고    scopus 로고
    • Novel chitosanase from Streptomyces griseus HUT 6037 with transglycosylation activity
    • Tanabe, T., K. Morinaga, T. Fukamizo, and M. Mitsutomi. 2003. Novel chitosanase from Streptomyces griseus HUT 6037 with transglycosylation activity. Biosci. Biotechnol. Biochem. 67: 354-364.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 354-364
    • Tanabe, T.1    Morinaga, K.2    Fukamizo, T.3    Mitsutomi, M.4
  • 82
    • 0033065770 scopus 로고    scopus 로고
    • Selective N-deacetylation of p-nitrophenyl N, N′-diacetyl-β-chitobioside and its use to differentiate the action of two types of chitinases
    • Tokuyasu, K., H. Ono, Y. Kitagawa, M. Ohnishi-Kameyama, K. Hayashi, and Y. Mori. 1999. Selective N-deacetylation of p-nitrophenyl N, N′-diacetyl-β-chitobioside and its use to differentiate the action of two types of chitinases. Carbohydr. Res. 316: 173-178.
    • (1999) Carbohydr. Res , vol.316 , pp. 173-178
    • Tokuyasu, K.1    Ono, H.2    Kitagawa, Y.3    Ohnishi-Kameyama, M.4    Hayashi, K.5    Mori, Y.6
  • 83
    • 0345374008 scopus 로고    scopus 로고
    • Preparation and characterisation of oligosaccharides produced by nitrous acid depolymerisation of chitosans
    • Tømmeraas, K., K. M. Vårum, B. E. Christensen, and O. Smidsrød. 2001. Preparation and characterisation of oligosaccharides produced by nitrous acid depolymerisation of chitosans. Carbohydr. Res. 333: 137-144.
    • (2001) Carbohydr. Res , vol.333 , pp. 137-144
    • Tømmeraas, K.1    Vårum, K.M.2    Christensen, B.E.3    Smidsrød, O.4
  • 84
    • 24044542341 scopus 로고    scopus 로고
    • Advances in understanding bioactivity of chitosan and chitosan oligomers against selected wood-inhabiting fungi
    • Torr, K. M., C. Chittenden, R. A. Franich, and B. Kreber. 2005. Advances in understanding bioactivity of chitosan and chitosan oligomers against selected wood-inhabiting fungi. Holzforschung 59: 559-567.
    • (2005) Holzforschung , vol.59 , pp. 559-567
    • Torr, K.M.1    Chittenden, C.2    Franich, R.A.3    Kreber, B.4
  • 85
    • 48449085799 scopus 로고    scopus 로고
    • Chemical preparation and structural characterization of a homogeneous series of chitin/chitosan oligomers
    • Trombotto, S., C. Ladaviere, F. Delolme, and A. Domard. 2008. Chemical preparation and structural characterization of a homogeneous series of chitin/chitosan oligomers. Biomacromolecules 9: 1731-1738.
    • (2008) Biomacromolecules , vol.9 , pp. 1731-1738
    • Trombotto, S.1    Ladaviere, C.2    Delolme, F.3    Domard, A.4
  • 86
    • 0942276366 scopus 로고    scopus 로고
    • Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-δ-lactone
    • Vaaje-Kolstad, G., A. Vasella, M. G. Peter et al. 2004. Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-δ-lactone. J. Biol. Chem. 279: 3612-3619.
    • (2004) J. Biol. Chem , vol.279 , pp. 3612-3619
    • Vaaje-Kolstad, G.1    Vasella, A.2    Peter, M.G.3
  • 87
    • 1942469296 scopus 로고    scopus 로고
    • Binding of the AVR4 elicitor of Cladosporium fulvum to chitotriose units is facilitated by positive allosteric protein-protein interactions: The chitin-binding site of AVR4 represents a novel binding site on the folding scaffold shared between the invertebrate and the plant chitin-binding domain
    • van den Burg, H. A., C. Spronk, S. Boeren et al. 2004. Binding of the AVR4 elicitor of Cladosporium fulvum to chitotriose units is facilitated by positive allosteric protein-protein interactions: The chitin-binding site of AVR4 represents a novel binding site on the folding scaffold shared between the invertebrate and the plant chitin-binding domain. J. Biol. Chem. 279: 16786-16796.
    • (2004) J. Biol. Chem , vol.279 , pp. 16786-16796
    • Van den Burg, H.A.1    Spronk, C.2    Boeren, S.3
  • 88
    • 0032009299 scopus 로고    scopus 로고
    • Mass spectrometric analysis of lipo-chitin oligosaccharides signal molecules mediating the host-specific legume-rhizobium symbiosis
    • Van der Drift, K. M. G. M., M. M. A. Olsthoorn, L. P. Brull, L. Blok-Tip, and J. E. Thomas-Oates. 1998. Mass spectrometric analysis of lipo-chitin oligosaccharides signal molecules mediating the host-specific legume-rhizobium symbiosis. Mass Spectrom. Rev. 17: 75-95.
    • (1998) Mass Spectrom. Rev , vol.17 , pp. 75-95
    • Van der Drift, K.M.G.M.1    Olsthoorn, M.M.A.2    Brull, L.P.3    Blok-Tip, L.4    Thomas-Oates, J.E.5
  • 89
    • 0026413044 scopus 로고
    • Determination of degree of N-acetylation and the distribution of N-acetyl groups in partially N-deacetylated chitins (Chitosans) by high field NMR spectroscopy
    • Vårum, K. M., M. W. Anthonsen, H. Grasdalen, and O. Smidsrød. 1991a. Determination of degree of N-acetylation and the distribution of N-acetyl groups in partially N-deacetylated chitins (chitosans) by high field NMR spectroscopy. Carbohydr. Res. 211: 17-23.
    • (1991) Carbohydr. Res , vol.211 , pp. 17-23
    • Vårum, K.M.1    Anthonsen, M.W.2    Grasdalen, H.3    Smidsrød, O.4
  • 92
    • 28044451541 scopus 로고    scopus 로고
    • Characterization of an exochitinase from Epiphyas postvittana nucleopolyhedrovirus (Family Baculoviridae)
    • Young, V. L., R. M. Simpson, and V. K. Ward. 2005. Characterization of an exochitinase from Epiphyas postvittana nucleopolyhedrovirus (family Baculoviridae). J. Gen. Virol. 86: 3253-3261.
    • (2005) J. Gen. Virol , vol.86 , pp. 3253-3261
    • Young, V.L.1    Simpson, R.M.2    Ward, V.K.3
  • 93
    • 33846453967 scopus 로고    scopus 로고
    • Electron detachment dissociation of glycosaminoglycan tetrasaccharides
    • Wolff, J. J., I. J. Amster, L. L. Chi, and R. J. Linhardt. 2007. Electron detachment dissociation of glycosaminoglycan tetrasaccharides. J. Am. Soc. Mass Spectrom. 18: 234-244.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 234-244
    • Wolff, J.J.1    Amster, I.J.2    Chi, L.L.3    Linhardt, R.J.4
  • 94
    • 33748475886 scopus 로고    scopus 로고
    • Structural monitoring of oligosaccharides through C-13 enrichment and NMR observation of acetyl groups
    • Yu, F. and J. H. Prestegard. 2006. Structural monitoring of oligosaccharides through C-13 enrichment and NMR observation of acetyl groups. Biophys. J. 91: 1952-1959.
    • (2006) Biophys. J , vol.91 , pp. 1952-1959
    • Yu, F.1    Prestegard, J.H.2
  • 95
    • 0032848260 scopus 로고    scopus 로고
    • Preparation of chitooligosaccharides from chitosan by a complex enzyme
    • Zhang, H., Y. G. Du, X. J. Yu, M. Mitsutomi, and S. Aiba. 1999. Preparation of chitooligosaccharides from chitosan by a complex enzyme. Carbohydr. Res. 320: 257-260.
    • (1999) Carbohydr. Res , vol.320 , pp. 257-260
    • Zhang, H.1    Du, Y.G.2    Yu, X.J.3    Mitsutomi, M.4    Aiba, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.