메뉴 건너뛰기




Volumn 23, Issue 6, 2013, Pages 1147-1155

Kinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: A fluorescence and surface plasmon resonance spectroscopic study

Author keywords

Holothuria scabra; Kinetic analysis; Lectin; Surface plasmon resonance spectroscopy; Thermodynamic properties

Indexed keywords

ANTI-BACTERIAL ACTIVITY; BIOLOGICAL IMPLICATIONS; HOLOTHURIA SCABRA; KINETIC ANALYSIS; KINETICS AND THERMODYNAMICS; LECTIN; SURFACE PLASMON RESONANCE SPECTROSCOPY; THERMODYNAMIC AND KINETIC ANALYSIS;

EID: 84886802927     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-013-1244-4     Document Type: Article
Times cited : (2)

References (44)
  • 1
    • 0026527649 scopus 로고
    • Invertebrate immunity: Another viewpoint
    • 1535984 10.1111/j.1365-3083.1992.tb02857.x 1:CAS:528:DyaK38XksVKjt7g%3D
    • Cooper EL, Rinkevich B, Uhlenbruck G, Valembois P (1992) Invertebrate immunity: another viewpoint. Scand J Immunol 35:247-266
    • (1992) Scand J Immunol , vol.35 , pp. 247-266
    • Cooper, E.L.1    Rinkevich, B.2    Uhlenbruck, G.3    Valembois, P.4
  • 3
    • 0002645734 scopus 로고
    • Bacterioplankton growth in sea water. 1. Growth kinetics and cellular characteristics in seawater cultures
    • 10.3354/meps018031
    • Ammerman JW, Fuhrman JA, Hagstrom A, Azam F (1984) Bacterioplankton growth in sea water. 1. Growth kinetics and cellular characteristics in seawater cultures. Mar Ecol Prog Ser 18:31-39
    • (1984) Mar Ecol Prog ser , vol.18 , pp. 31-39
    • Ammerman, J.W.1    Fuhrman, J.A.2    Hagstrom, A.3    Azam, F.4
  • 4
    • 0001369441 scopus 로고
    • Phagocytosis and non-self recognition in invertebrates
    • 10.2307/1311504
    • Bayne CJ (1990) Phagocytosis and non-self recognition in invertebrates. Bioscience 40:723-731
    • (1990) Bioscience , vol.40 , pp. 723-731
    • Bayne, C.J.1
  • 5
    • 0029916815 scopus 로고    scopus 로고
    • Antibacterial activity in the coelomocyte of the sea urchin Paracentrotus lividus
    • 10.1016/0305-0491(95)02080-2 1:CAS:528:DyaK28Xit1Oqtro%3D
    • Stabili I, Pagliara P, Roch P (1996) Antibacterial activity in the coelomocyte of the sea urchin Paracentrotus lividus. Comp Biochem Phys 113B:639-644
    • (1996) Comp Biochem Phys , vol.113 , pp. 639-644
    • Stabili, I.1    Pagliara, P.2    Roch, P.3
  • 6
    • 0002199711 scopus 로고
    • The lectins: Properties, functions, and applications in biology and medicine
    • N. Sharon I.J. Goldstein (eds) Academic New York
    • Goldstein IJ, Poretz RD (1986) The lectins: properties, functions, and applications in biology and medicine. In: Sharon N, Goldstein IJ (eds) Liener IE. Academic, New York, pp 33-247
    • (1986) Liener IE , pp. 33-247
    • Goldstein, I.J.1    Poretz, R.D.2
  • 7
    • 0022555853 scopus 로고
    • Lectins as molecules and as tools
    • 3527046 10.1146/annurev.bi.55.070186.000343 1:CAS:528:DyaL28XkvFGlsro%3D
    • Lis H, Sharon N (1986) Lectins as molecules and as tools. Annu Rev Biochem 55:35-67
    • (1986) Annu Rev Biochem , vol.55 , pp. 35-67
    • Lis, H.1    Sharon, N.2
  • 8
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • 2552581 10.1126/science.2552581 1:CAS:528:DyaK3cXis1Gr
    • Sharon N, Lis H (1989) Lectins as cell recognition molecules. Science 246:227-234
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 9
    • 0000186025 scopus 로고
    • Tipson PS, Horton D (eds) Academic press, New York
    • Goldstein IJ, Hayes CE (1978) In: Tipson PS, Horton D (eds) Adv Carbohyd Chem Biochem 35: Academic press, New York pp 128-165
    • (1978) Adv Carbohyd Chem Biochem , vol.35 , pp. 128-165
    • Goldstein, I.J.1    Hayes, C.E.2
  • 10
    • 52049098247 scopus 로고    scopus 로고
    • T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): Possible involvement in differential recognition of bacteria
    • 10.1016/j.jip.2008.04.003 1:CAS:528:DC%2BD1cXhtFektrzM
    • Gowda NM, Goswami U, Khan MI (2008) T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): Possible involvement in differential recognition of bacteria. J Invert Pathol 99:141-145
    • (2008) J Invert Pathol , vol.99 , pp. 141-145
    • Gowda, N.M.1    Goswami, U.2    Khan, M.I.3
  • 11
    • 40149087683 scopus 로고    scopus 로고
    • Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)
    • 10.1016/j.fsi.2008.01.002 1:CAS:528:DC%2BD1cXjtVels7k%3D
    • Gowda NM, Goswami U, Khan MI (2008) Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra). Fish and shellfish Immunol 24:450-458
    • (2008) Fish and Shellfish Immunol. , vol.24 , pp. 450-458
    • Gowda, N.M.1    Goswami, U.2    Khan, M.I.3
  • 12
    • 0034856563 scopus 로고    scopus 로고
    • Thomsen-Friedenreich (T) antigen: A possible tool for differentiating sebaceous carcinoma from its simulators
    • 11556753 10.1097/00022744-200109000-00009 1:STN:280: DC%2BD3Mrgslyitw%3D%3D
    • Hassanein AM, Al-Quran SZ, Kantor GR, Pauporte M, Telang GH, Spielvogel RL (2001) Thomsen-Friedenreich (T) antigen: a possible tool for differentiating sebaceous carcinoma from its simulators. Appl Immunohistochem Mol Morphol 9:250-254
    • (2001) Appl Immunohistochem Mol Morphol , vol.9 , pp. 250-254
    • Hassanein, A.M.1    Al-Quran, S.Z.2    Kantor, G.R.3    Pauporte, M.4    Telang, G.H.5    Spielvogel, R.L.6
  • 13
    • 0031822453 scopus 로고    scopus 로고
    • Differential expression of the cancer associated antigens T (Thomsen-Friedenreich) and Tn to the skin in primary and metastatic carcinomas
    • 9828816 10.1136/jcp.51.8.588 1:STN:280:DyaK1M%2Fks1amtA%3D%3D
    • Kanitakis J, al-Rifai I, Faure M, Claudy A (1998) Differential expression of the cancer associated antigens T (Thomsen-Friedenreich) and Tn to the skin in primary and metastatic carcinomas. J Clin Pathol 51:588-592
    • (1998) J Clin Pathol , vol.51 , pp. 588-592
    • Kanitakis, J.1    Al-Rifai, I.2    Faure, M.3    Claudy, A.4
  • 14
    • 0142242217 scopus 로고    scopus 로고
    • Identification of the sea urchin 350-kDa sperm-binding protein as a new sialic acid binding lectin that belongs to the heat shock protein 110 family
    • 12917406 10.1074/jbc.M307493200 1:CAS:528:DC%2BD3sXot1amt7Y%3D
    • Maehashi E, Sato C, Ohta K et al (2003) Identification of the sea urchin 350-kDa sperm-binding protein as a new sialic acid binding lectin that belongs to the heat shock protein 110 family. J Biol Chem 278:42050-42057
    • (2003) J Biol Chem , vol.278 , pp. 42050-42057
    • Maehashi, E.1    Sato, C.2    Ohta, K.3
  • 15
    • 0026734267 scopus 로고
    • Developmental expression of ehinonectin, an endogenous lectin of the sea urchin embryo
    • 10.1111/j.1440-169X.1992.tb00003.x 1:CAS:528:DyaK38Xlt1yntr8%3D
    • Fuhrman MH, Suhan JP, Ettensohn CA (1992) Developmental expression of ehinonectin, an endogenous lectin of the sea urchin embryo. Develop Growth and Differ 34:137-150
    • (1992) Develop Growth and Differ , vol.34 , pp. 137-150
    • Fuhrman, M.H.1    Suhan, J.P.2    Ettensohn, C.A.3
  • 16
    • 0026750960 scopus 로고
    • Lectins in the hemolymph of the a starfish, Asterina pectinifera: Purification and characterization
    • 1499841 10.1016/0145-305X(92)90023-6 1:CAS:528:DyaK38XltV2qsrY%3D
    • Kamiya H, Muramoto K, Goto R, Sakai M (1992) Lectins in the hemolymph of the a starfish, Asterina pectinifera: purification and characterization. Dev Comp Immunol 16:243-250
    • (1992) Dev Comp Immunol , vol.16 , pp. 243-250
    • Kamiya, H.1    Muramoto, K.2    Goto, R.3    Sakai, M.4
  • 18
    • 77953974373 scopus 로고    scopus 로고
    • SUEL-related lectins, a lectin family widely distributed throughout organisms
    • 10.1271/bbb.100086
    • Tateno H (2010) SUEL-related lectins, a lectin family widely distributed throughout organisms. Biosci Biotechnol Biochem 74:141-1144
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 141-1144
    • Tateno, H.1
  • 20
    • 0034241026 scopus 로고    scopus 로고
    • Isolation and properties of a mannan-binding lectin from the coelomic fluid of the holothurian Cucumaria japonica
    • 1:CAS:528:DC%2BD3cXosVGmurk%3D
    • Bulgakov AA, Nazarenko EL, Petrova IY, Eliseikina MG, Vakhrusheva NM et al (2000) Isolation and properties of a mannan-binding lectin from the coelomic fluid of the holothurian Cucumaria japonica. Biochemistry (Mosco) 65:933-939
    • (2000) Biochemistry (Mosco) , vol.65 , pp. 933-939
    • Bulgakov, A.A.1    Nazarenko, E.L.2    Petrova, I.Y.3    Eliseikina, M.G.4    Vakhrusheva, N.M.5
  • 21
    • 0028171441 scopus 로고
    • 2+-dependent lectins from coelomic plasma of sea cucumber, Stichopus japonicas
    • 7896742 1:CAS:528:DyaK2MXislCjtLw%3D
    • 2+-dependent lectins from coelomic plasma of sea cucumber, Stichopus japonicas. J Biochem 116:1127-1133
    • (1994) J Biochem , vol.116 , pp. 1127-1133
    • Matsui, T.1    Ozeki, Y.2    Suzuki, M.3    Hino, A.4    Titani, K.5
  • 22
    • 85004613200 scopus 로고
    • Purification and characterization of two lectins from the sea cucumber, Stichopus japonicas
    • 10.1271/bbb.57.1736
    • Hatakeyama T, Kohzaki H, Nagatomo H, Yamasaki N (1994) Purification and characterization of two lectins from the sea cucumber, Stichopus japonicas. Biosci Biotechnol Biochem 57:1736-1739
    • (1994) Biosci Biotechnol Biochem , vol.57 , pp. 1736-1739
    • Hatakeyama, T.1    Kohzaki, H.2    Nagatomo, H.3    Yamasaki, N.4
  • 23
    • 0004838347 scopus 로고
    • Hemagglutinin and hemolysin levels in the coelomic fluid from Holothuria polii (Echinodermata) following sheep erythrocyte injection
    • 10.2307/1541182
    • Canicatti C, Parrinello N (1985) Hemagglutinin and hemolysin levels in the coelomic fluid from Holothuria polii (Echinodermata) following sheep erythrocyte injection. Biol Bull 168:175-182
    • (1985) Biol Bull , vol.168 , pp. 175-182
    • Canicatti, C.1    Parrinello, N.2
  • 24
    • 84954969816 scopus 로고
    • Naturally occurring hemagglutinins in the coelomic fluid of the Echinoderms Holothuria polii Delle Chiaje and Holothuria tubulosa Gmelin
    • Parrinello N, Canicatti C, Rindone D (1976) Naturally occurring hemagglutinins in the coelomic fluid of the Echinoderms Holothuria polii Delle Chiaje and Holothuria tubulosa Gmelin. Biol Bull 43:259-271
    • (1976) Biol Bull , vol.43 , pp. 259-271
    • Parrinello, N.1    Canicatti, C.2    Rindone, D.3
  • 25
    • 79953166038 scopus 로고    scopus 로고
    • Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif
    • 21247895 10.1074/jbc.M110.200576 1:CAS:528:DC%2BC3MXjsVyrurY%3D
    • Hatakeyama T, Kamiya T, Kusunoki M, Nakamura-Tsuruta S, Hirabayashi J et al (2011) Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif. J Biol Chem 286:10305-10315
    • (2011) J Biol Chem , vol.286 , pp. 10305-10315
    • Hatakeyama, T.1    Kamiya, T.2    Kusunoki, M.3    Nakamura-Tsuruta, S.4    Hirabayashi, J.5
  • 26
    • 0030959108 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in studies of carbohydrate-protein interactions
    • 10.1093/oxfordjournals.jbchem.a021658 1:CAS:528:DyaK2sXjvV2gs70%3D
    • Lee YC (1997) Fluorescence spectroscopy in studies of carbohydrate-protein interactions. J Biochem (Tokyo) 121:818-825
    • (1997) J Biochem (Tokyo) , vol.121 , pp. 818-825
    • Lee, Y.C.1
  • 27
    • 0003054945 scopus 로고
    • Methods for measuring the affinity between carbohydrate ligands and certain proteins
    • 1:CAS:528:DyaL3cXmtVShs7k%3D
    • Glaudemans CPJ (1980) Methods for measuring the affinity between carbohydrate ligands and certain proteins. Methods Carbohydr Chem 8:145-149
    • (1980) Methods Carbohydr Chem , vol.8 , pp. 145-149
    • Glaudemans, C.P.J.1
  • 28
    • 0027521218 scopus 로고
    • Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance
    • 10.1038/365343a0
    • Schuster SC, Swanson RV, Alex LA, Bourret RB, Simon MI (1993) Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance. Nature 365:347-351
    • (1993) Nature , vol.365 , pp. 347-351
    • Schuster, S.C.1    Swanson, R.V.2    Alex, L.A.3    Bourret, R.B.4    Simon, M.I.5
  • 29
    • 0023055761 scopus 로고
    • Binding of N-linked bovine fetuin glycopeptides to isolated rabbit erythrocytes: Gal/GalNAc hepatic lectin discrimination between Galβ (1,4) GlcNAc and Galβ (1,3) GlcNAc in a triantennary structure
    • 2430615 10.1021/bi00367a055 1:CAS:528:DyaL28XlsFSgtrk%3D
    • Townsend RR, Hardy MR, Wong TC, Lee YC (1986) Binding of N-linked bovine fetuin glycopeptides to isolated rabbit erythrocytes: Gal/GalNAc hepatic lectin discrimination between Gal.beta (1,4) GlcNAc and Gal.beta (1,3) GlcNAc in a triantennary structure. Biochemistry 25:5716-5725
    • (1986) Biochemistry , vol.25 , pp. 5716-5725
    • Townsend, R.R.1    Hardy, M.R.2    Wong, T.C.3    Lee, Y.C.4
  • 30
    • 0014010208 scopus 로고    scopus 로고
    • Soybean hemagglutinin a plant glycoprotein: Isolation of glycopeptides
    • Lis H, Sharon N, Katchalski (1996) Soybean hemagglutinin a plant glycoprotein: Isolation of glycopeptides. J Biol Chem 241: 684-689
    • (1996) J Biol Chem , vol.241 , pp. 684-689
    • Lis, H.1    Sharon, N.K.2
  • 31
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • 10.1021/ac60111a017 1:CAS:528:DyaG28XjvFynsg%3D%3D
    • Dubois M, Gills KK, Hamilton JK, Rebers PA, Smoth F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gills, K.K.2    Hamilton, J.K.3    Rebers, P.A.4    Smoth, F.5
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 77950865952 scopus 로고    scopus 로고
    • Fluorescence quenching to study protein-ligand binding: Common errors
    • 19997966 10.1007/s10895-009-0572-x
    • van de Weert M (2010) Fluorescence quenching to study protein-ligand binding: common errors. J Fluoresc 20:625-629
    • (2010) J Fluoresc , vol.20 , pp. 625-629
    • Van De Weert, M.1
  • 34
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • 10.1016/j.molstruc.2011.05.023
    • van de Weert M, Stella L (2011) Fluorescence quenching and ligand binding: a critical discussion of a popular methodology. J Mol Struct 998:144-150
    • (2011) J Mol Struct , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2
  • 35
    • 0014199062 scopus 로고
    • The binding of oligosaccharides containing N-acetylglucosamine and N- acetylmuramic acid to lysozyme. The specificity of binding subsites
    • 6070843 1:CAS:528:DyaF2sXkvFOitbs%3D
    • Chipman DM, Grisaro V, Sharon N (1967) The binding of oligosaccharides containing N-acetylglucosamine and N- acetylmuramic acid to lysozyme. The specificity of binding subsites. J Biol Chem 242:4388-4394
    • (1967) J Biol Chem , vol.242 , pp. 4388-4394
    • Chipman, D.M.1    Grisaro, V.2    Sharon, N.3
  • 36
    • 33846001280 scopus 로고    scopus 로고
    • Purification and characterization of a lectin from endophytic fungus Fusarium solani having complex sugar specificity
    • 17118333 10.1016/j.abb.2006.10.019 1:CAS:528:DC%2BD2sXmtVGgsw%3D%3D
    • Khan F, Ahmad A, Khan MI (2007) Purification and characterization of a lectin from endophytic fungus Fusarium solani having complex sugar specificity. Arch Biochem Biophys 457:243-251
    • (2007) Arch Biochem Biophys , vol.457 , pp. 243-251
    • Khan, F.1    Ahmad, A.2    Khan, M.I.3
  • 37
    • 39749189527 scopus 로고    scopus 로고
    • Complex carbohydrate specificity of lectin from fruiting body of Ganoderma lucidum. A surface plasmon study
    • 17917934 10.1080/15216540701663463 1:CAS:528:DC%2BD2sXhsVent7zO
    • Thakur A, Pal L, Ahmad A, Khan MI (2007) Complex carbohydrate specificity of lectin from fruiting body of Ganoderma lucidum. A surface plasmon study. IUBMB Life 59:758-764
    • (2007) IUBMB Life , vol.59 , pp. 758-764
    • Thakur, A.1    Pal, L.2    Ahmad, A.3    Khan, M.I.4
  • 38
    • 0034691312 scopus 로고    scopus 로고
    • Near-ultraviolet magnetic circular dichroism spectroscopy of protein conformational states: Correlation of tryptophan band position and intensity with hemoglobin allostery
    • 10852712 10.1021/bi992823a 1:CAS:528:DC%2BD3cXjtFygt7s%3D
    • Vitale DJ, Goldbeck RA, Kim-Shapiro DB, Esquerra RM, Parkhurst LJ, Kliger DS (2000) Near-ultraviolet magnetic circular dichroism spectroscopy of protein conformational states: correlation of tryptophan band position and intensity with hemoglobin allostery. Biochemistry 39:7145-7152
    • (2000) Biochemistry , vol.39 , pp. 7145-7152
    • Vitale, D.J.1    Goldbeck, R.A.2    Kim-Shapiro, D.B.3    Esquerra, R.M.4    Parkhurst, L.J.5    Kliger, D.S.6
  • 39
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • 12369905 10.2174/1389203003381315 1:CAS:528:DC%2BD3MXns1ehtw%3D%3D
    • Kelly SM, Price NC (2000) The use of circular dichroism in the investigation of protein structure and function. Curr Protein Pept Sci 1:349-384
    • (2000) Curr Protein Pept Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 40
    • 0027484964 scopus 로고
    • Binding of the O-antigen of Shigella dysenteriae type 1 and 26 related synthetic fragments to a monoclonal IgM antibody
    • 7503987 1:CAS:528:DyaK3sXmt1eku70%3D
    • Pavliak V, Nashed EM, Pozsgay V, Kovac P, Karpas A et al (1993) Binding of the O-antigen of Shigella dysenteriae type 1 and 26 related synthetic fragments to a monoclonal IgM antibody. J Biol Chem 268:25797-25779
    • (1993) J Biol Chem , vol.268 , pp. 25797-25779
    • Pavliak, V.1    Nashed, E.M.2    Pozsgay, V.3    Kovac, P.4    Karpas, A.5
  • 41
    • 0005872506 scopus 로고    scopus 로고
    • The structure of the carbohydrate backbones of the lipopolysaccharides from Escherichia coli rough mutants F470 (R1 core type) and F576 (R2 core type)
    • 10215878 10.1046/j.1432-1327.1999.00280.x 1:CAS:528:DyaK1MXjtFClt7s%3D
    • Vinogradov EV, Drift KV, Thomas-Oates JE, Meshkov S, Brade H, Holst O (1999) The structure of the carbohydrate backbones of the lipopolysaccharides from Escherichia coli rough mutants F470 (R1 core type) and F576 (R2 core type). Eur J Biochem 261:629-639
    • (1999) Eur J Biochem , vol.261 , pp. 629-639
    • Vinogradov, E.V.1    Drift, K.V.2    Thomas-Oates, J.E.3    Meshkov, S.4    Brade, H.5    Holst, O.6
  • 42
    • 0031754994 scopus 로고    scopus 로고
    • Applications of lectins and neoglycoconjugates in histology and pathology
    • 9780360 10.1159/000046459 1:CAS:528:DyaK1cXntVektrY%3D
    • Danguy A, Decaestecker C, Genten F, Salmon I, Kiss R (1998) Applications of lectins and neoglycoconjugates in histology and pathology. Acta Anatomica 161:206-218
    • (1998) Acta Anatomica , vol.161 , pp. 206-218
    • Danguy, A.1    Decaestecker, C.2    Genten, F.3    Salmon, I.4    Kiss, R.5
  • 43
    • 0017610878 scopus 로고
    • Binding of 4-methylumbelliferyl [alpha]-D-mannopyranoside to dimeric concavalin A: Fluorescence temperature-jump relaxation study
    • 836782 10.1021/bi00621a002 1:CAS:528:DyaE2sXosFSitQ%3D%3D
    • Clegg RM, Loontiens FG, Jovin TM (1977) Binding of 4-methylumbelliferyl [alpha]-D-mannopyranoside to dimeric concavalin A: fluorescence temperature-jump relaxation study. Biochemistry 16:167-175
    • (1977) Biochemistry , vol.16 , pp. 167-175
    • Clegg, R.M.1    Loontiens, F.G.2    Jovin, T.M.3
  • 44
    • 0035937095 scopus 로고    scopus 로고
    • On the stringent requirement of mannosyl substitution in mannooligosaccharides for the recognition by garlic (Allium sativum) lectin. A surface plasmon resonance study
    • 11076955 10.1074/jbc.M009533200 1:CAS:528:DC%2BD3MXhs1KmsLo%3D
    • Bachhawat K, Thomas CJ, Amutha B, Krishnasastry MV, Khan MI et al (2001) On the stringent requirement of mannosyl substitution in mannooligosaccharides for the recognition by garlic (Allium sativum) lectin. A surface plasmon resonance study. J Biol Chem 276:5541-5546
    • (2001) J Biol Chem , vol.276 , pp. 5541-5546
    • Bachhawat, K.1    Thomas, C.J.2    Amutha, B.3    Krishnasastry, M.V.4    Khan, M.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.