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Volumn 14, Issue 1, 2014, Pages

Molecular analysis of hyperthermophilic endoglucanase Cel12B from Thermotoga maritima and the properties of its functional residues

Author keywords

Cellulose; Conserved amino acid residues; Endoglucanase; Phylogenetic analysis; Thermostability

Indexed keywords

AMINO ACID DERIVATIVE; BACTERIAL ENZYME; CYSTEINE; ENDOGLUCANASE CEL12B; GLUCAN SYNTHASE; HISTIDINE; NUCLEOPHILE; PROTON; UNCLASSIFIED DRUG;

EID: 84896733153     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-14-8     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 18044366388 scopus 로고    scopus 로고
    • Directed evolution for engineering pH profile of endoglucanase III from Trichoderma reesei
    • 15857788
    • Directed evolution for engineering pH profile of endoglucanase III from Trichoderma reesei. Wang T, Liu X, Yu Q, Zhang X, Qu Y, Gao P, Biomol Eng 2005 22 1-3 89 94 15857788
    • (2005) Biomol Eng , vol.22 , Issue.1-3 , pp. 89-94
    • Wang, T.1    Liu, X.2    Yu, Q.3    Zhang, X.4    Qu, Y.5    Gao, P.6
  • 2
    • 79957475689 scopus 로고    scopus 로고
    • Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile
    • 10.1016/j.jbiotec.2011.03.025 21501637
    • Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile. Liang C, Fioroni M, Rodriguez-Ropero F, Xue Y, Schwaneberg U, Ma Y, J Biotechnol 2011 154 1 46 53 10.1016/j.jbiotec.2011.03.025 21501637
    • (2011) J Biotechnol , vol.154 , Issue.1 , pp. 46-53
    • Liang, C.1    Fioroni, M.2    Rodriguez-Ropero, F.3    Xue, Y.4    Schwaneberg, U.5    Ma, Y.6
  • 3
    • 78650850328 scopus 로고    scopus 로고
    • Thermostability enhancement of Clostridium thermocellum cellulosomal endoglucanase Cel8A by a single glycine substitution
    • 10.1002/cctc.201000112
    • Thermostability enhancement of Clostridium thermocellum cellulosomal endoglucanase Cel8A by a single glycine substitution. Anbar M, Lamed R, Bayer EA, Chemcatchem 2010 2 8 997 1003 10.1002/cctc.201000112
    • (2010) Chemcatchem , vol.2 , Issue.8 , pp. 997-1003
    • Anbar, M.1    Lamed, R.2    Bayer, E.A.3
  • 4
    • 67349210640 scopus 로고    scopus 로고
    • Directed evolution of endoglucanase III (Cel12A) from trichoderma reesei
    • 10.1007/s00253-009-1901-3 19205687
    • Directed evolution of endoglucanase III (Cel12A) from trichoderma reesei. Nakazawa H, Okada K, Onodera T, Ogasawara W, Okada H, Morikawa Y, Appl Microbiol Biotechnol 2009 83 4 649 657 10.1007/s00253-009-1901-3 19205687
    • (2009) Appl Microbiol Biotechnol , vol.83 , Issue.4 , pp. 649-657
    • Nakazawa, H.1    Okada, K.2    Onodera, T.3    Ogasawara, W.4    Okada, H.5    Morikawa, Y.6
  • 5
    • 0032560853 scopus 로고    scopus 로고
    • A cellulase gene of termite origin
    • 10.1038/28527 9690469
    • A cellulase gene of termite origin. Watanabe H, Noda H, Tokuda G, Lo N, Nature 1998 394 6691 330 331 10.1038/28527 9690469
    • (1998) Nature , vol.394 , Issue.6691 , pp. 330-331
    • Watanabe, H.1    Noda, H.2    Tokuda, G.3    Lo, N.4
  • 6
    • 17744380000 scopus 로고    scopus 로고
    • Ancient origin of glycosyl hydrolase family 9 cellulase genes
    • 10.1093/molbev/msi107 15703240
    • Ancient origin of glycosyl hydrolase family 9 cellulase genes. Davison A, Mol Biol Evol 2005 22 5 1273 1284 10.1093/molbev/msi107 15703240
    • (2005) Mol Biol Evol , vol.22 , Issue.5 , pp. 1273-1284
    • Davison, A.1
  • 7
    • 77955974756 scopus 로고    scopus 로고
    • The genome sequence of the crenarchaeon Acidilobus saccharovorans supports a new order, Acidilobales, and suggests an important ecological role in terrestrial acidic hot Springs
    • 10.1128/AEM.00599-10 20581186
    • The genome sequence of the crenarchaeon Acidilobus saccharovorans supports a new order, Acidilobales, and suggests an important ecological role in terrestrial acidic hot Springs. Mardanov AV, Svetlitchnyi VA, Beletsky AV, Prokofeva MI, Bonch-Osmolovskaya EA, Ravin NV, Skryabin KG, Appl Environ Microbiol 2010 76 16 5652 5657 10.1128/AEM.00599-10 20581186
    • (2010) Appl Environ Microbiol , vol.76 , Issue.16 , pp. 5652-5657
    • Mardanov, A.V.1    Svetlitchnyi, V.A.2    Beletsky, A.V.3    Prokofeva, M.I.4    Bonch-Osmolovskaya, E.A.5    Ravin, N.V.6    Skryabin, K.G.7
  • 8
    • 66649087973 scopus 로고    scopus 로고
    • Biogeography of the Sulfolobus islandicus pan-genome
    • 10.1073/pnas.0808945106 19435847
    • Biogeography of the Sulfolobus islandicus pan-genome. Reno ML, Held NL, Fields CJ, Burke PV, Whitaker RJ, Proc Natl Acad Sci 2009 106 21 8605 8610 10.1073/pnas.0808945106 19435847
    • (2009) Proc Natl Acad Sci , vol.106 , Issue.21 , pp. 8605-8610
    • Reno, M.L.1    Held, N.L.2    Fields, C.J.3    Burke, P.V.4    Whitaker, R.J.5
  • 9
    • 79952803560 scopus 로고    scopus 로고
    • Genome analyses of Icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies
    • 10.1128/JB.01487-10 21278296
    • Genome analyses of Icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies. Guo L, Brugger K, Liu C, Shah SA, Zheng H, Zhu Y, Wang S, Lillestol RK, Chen L, Frank J, et al. J Bacteriol 2011 193 7 1672 1680 10.1128/JB.01487-10 21278296
    • (2011) J Bacteriol , vol.193 , Issue.7 , pp. 1672-1680
    • Guo, L.1    Brugger, K.2    Liu, C.3    Shah, S.A.4    Zheng, H.5    Zhu, Y.6    Wang, S.7    Lillestol, R.K.8    Chen, L.9    Frank, J.10
  • 11
    • 78649660338 scopus 로고    scopus 로고
    • Genome sequence of the polysaccharide-degrading, thermophilic anaerobe Spirochaeta thermophila DSM 6192
    • 10.1128/JB.01023-10 20935097
    • Genome sequence of the polysaccharide-degrading, thermophilic anaerobe Spirochaeta thermophila DSM 6192. Angelov A, Liebl S, Ballschmiter M, Boemeke M, Lehmann R, Liesegang H, Daniel R, Liebl W, J Bacteriol 2010 192 24 6492 6493 10.1128/JB.01023-10 20935097
    • (2010) J Bacteriol , vol.192 , Issue.24 , pp. 6492-6493
    • Angelov, A.1    Liebl, S.2    Ballschmiter, M.3    Boemeke, M.4    Lehmann, R.5    Liesegang, H.6    Daniel, R.7    Liebl, W.8
  • 14
    • 79959364251 scopus 로고    scopus 로고
    • Complete genome sequence of Metallosphaera cuprina, a metal sulfide-oxidizing archaeon from a hot spring
    • 10.1128/JB.05038-11 21551305
    • Complete genome sequence of Metallosphaera cuprina, a metal sulfide-oxidizing archaeon from a hot spring. Liu L-J, You X-Y, Zheng H, Wang S, Jiang C-Y, Liu S-J, J Bacteriol 2011 193 13 3387 3388 10.1128/JB.05038-11 21551305
    • (2011) J Bacteriol , vol.193 , Issue.13 , pp. 3387-3388
    • Liu, L.-J.1    You, X.-Y.2    Zheng, H.3    Wang, S.4    Jiang, C.-Y.5    Liu, S.-J.6
  • 16
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes. Liebl W, Ruile P, Bronnenmeier K, Riedel K, Lottspeich F, Greif I, Microbiol (Reading, England) 1996 142 Pt 9 2533 2542
    • (1996) Microbiol (Reading, England) , vol.142 , Issue.PART 9 , pp. 2533-2542
    • Liebl, W.1    Ruile, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 18
    • 43349089243 scopus 로고    scopus 로고
    • Inferring evolutionary trees with PAUP
    • Chaper 6, unit 6.4. http://www.currentprotocols.com/protocol/bi0604
    • Inferring evolutionary trees with PAUP. Wilgenbusch JC, Swofford D, Curr Protoc Bioinformatics 2003 Chaper 6, unit 6.4. http://www.currentprotocols.com/ protocol/bi0604
    • (2003) Curr Protoc Bioinformatics
    • Wilgenbusch, J.C.1    Swofford, D.2
  • 19
    • 0036154307 scopus 로고    scopus 로고
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides
    • 10.1128/AEM.68.2.545-554.2002 11823189
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Chhabra SR, Shockley KR, Ward DE, Kelly RM, Appl Environ Microbiol 2002 68 2 545 554 10.1128/AEM.68.2.545-554.2002 11823189
    • (2002) Appl Environ Microbiol , vol.68 , Issue.2 , pp. 545-554
    • Chhabra, S.R.1    Shockley, K.R.2    Ward, D.E.3    Kelly, R.M.4
  • 20
    • 84866177781 scopus 로고    scopus 로고
    • A novel thermostable cellulase from Fervidobacterium nodosum
    • A novel thermostable cellulase from Fervidobacterium nodosum. Wang Y, Wang X, Tang R, Yu S, Zheng B, Feng Y, J Mol Catal B Enzym 2010 66 3-4 294 301
    • (2010) J Mol Catal B Enzym , vol.66 , Issue.3-4 , pp. 294-301
    • Wang, Y.1    Wang, X.2    Tang, R.3    Yu, S.4    Zheng, B.5    Feng, Y.6
  • 21
    • 11944256494 scopus 로고
    • Catalyic mechanisms of enzymatic glycosyl transfer
    • 10.1021/cr00105a006
    • Catalyic mechanisms of enzymatic glycosyl transfer. Sinnott ML, Chem Rev 1990 90 7 1171 1202 10.1021/cr00105a006
    • (1990) Chem Rev , vol.90 , Issue.7 , pp. 1171-1202
    • Sinnott, M.L.1
  • 22
    • 0141828152 scopus 로고    scopus 로고
    • Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins
    • 10.1038/nature01977 13679914
    • Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins. Gaucher EA, Thomson JM, Burgan MF, Benner SA, Nature 2003 425 6955 285 288 10.1038/nature01977 13679914
    • (2003) Nature , vol.425 , Issue.6955 , pp. 285-288
    • Gaucher, E.A.1    Thomson, J.M.2    Burgan, M.F.3    Benner, S.A.4
  • 23
    • 67649603168 scopus 로고    scopus 로고
    • Metabolic versatility and Indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis
    • 10.1128/AEM.00718-09 19447963
    • Metabolic versatility and Indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis. Mardanov AV, Ravin NV, Svetlitchnyi VA, Beletsky AV, Miroshnichenko ML, Bonch-Osmolovskaya EA, Skryabin KG, Appl Environ Microbiol 2009 75 13 4580 4588 10.1128/AEM.00718-09 19447963
    • (2009) Appl Environ Microbiol , vol.75 , Issue.13 , pp. 4580-4588
    • Mardanov, A.V.1    Ravin, N.V.2    Svetlitchnyi, V.A.3    Beletsky, A.V.4    Miroshnichenko, M.L.5    Bonch-Osmolovskaya, E.A.6    Skryabin, K.G.7
  • 24
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • 10.1093/protein/13.3.179 10775659
    • Factors enhancing protein thermostability. Kumar S, Tsai CJ, Nussinov R, Protein Eng 2000 13 3 179 191 10.1093/protein/13.3.179 10775659
    • (2000) Protein Eng , vol.13 , Issue.3 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 25
    • 0029591937 scopus 로고
    • Composition analysis of alpha-helices in thermophilic organisms
    • 10.1093/protein/8.9.905 8746728
    • Composition analysis of alpha-helices in thermophilic organisms. Warren GL, Petsko GA, Protein Eng 1995 8 9 905 913 10.1093/protein/8.9.905 8746728
    • (1995) Protein Eng , vol.8 , Issue.9 , pp. 905-913
    • Warren, G.L.1    Petsko, G.A.2
  • 26
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting alpha-helices: Position-specific analysis of alpha-helices in globular proteins
    • 10.1002/(SICI)1097-0134(19980601)31:4<460: AID-PROT12>3.0.CO;2-D 9626705
    • Dissecting alpha-helices: position-specific analysis of alpha-helices in globular proteins. Kumar S, Bansal M, Proteins 1998 31 4 460 476 10.1002/(SICI)1097-0134(19980601)31:4<460::AID-PROT12>3.0.CO;2-D 9626705
    • (1998) Proteins , vol.31 , Issue.4 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 27
    • 0026526263 scopus 로고
    • Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn
    • 1331044
    • Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. Kimura S, Kanaya S, Nakamura H, J Biol Chem 1992 267 31 22014 22017 1331044
    • (1992) J Biol Chem , vol.267 , Issue.31 , pp. 22014-22017
    • Kimura, S.1    Kanaya, S.2    Nakamura, H.3
  • 28
    • 0029670677 scopus 로고    scopus 로고
    • Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus
    • 10.1021/bi951581l 8573574
    • Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus. Kawamura S, Kakuta Y, Tanaka I, Hikichi K, Kuhara S, Yamasaki N, Kimura M, Biochemistry 1996 35 4 1195 1200 10.1021/bi951581l 8573574
    • (1996) Biochemistry , vol.35 , Issue.4 , pp. 1195-1200
    • Kawamura, S.1    Kakuta, Y.2    Tanaka, I.3    Hikichi, K.4    Kuhara, S.5    Yamasaki, N.6    Kimura, M.7
  • 29
    • 0029890431 scopus 로고    scopus 로고
    • Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues
    • 8787404
    • Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues. Watanabe K, Kitamura K, Suzuki Y, Appl Environ Microbiol 1996 62 6 2066 2073 8787404
    • (1996) Appl Environ Microbiol , vol.62 , Issue.6 , pp. 2066-2073
    • Watanabe, K.1    Kitamura, K.2    Suzuki, Y.3
  • 30
    • 0001767586 scopus 로고
    • A strong correlation between the increase in mumber of proline resdues and the rise in thermostability of 5 Bacillus oligo-1,6-glucsidases
    • 10.1007/BF00253030
    • A strong correlation between the increase in mumber of proline resdues and the rise in thermostability of 5 Bacillus oligo-1,6-glucsidases. Suzuki Y, Oishi K, Nakano H, Nagayama T, Appl Microbiol Biotechnol 1987 26 6 546 551 10.1007/BF00253030
    • (1987) Appl Microbiol Biotechnol , vol.26 , Issue.6 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 31
    • 0032867166 scopus 로고    scopus 로고
    • Increasing the thermostability of D-xylose isomerase by introduction of a proline into the turn of a random coil
    • 10.1093/protein/12.8.635 10469823
    • Increasing the thermostability of D-xylose isomerase by introduction of a proline into the turn of a random coil. Zhu GP, Xu C, Teng MK, Tao LM, Zhu XY, Wu CJ, Hang J, Niu LW, Wang YZ, Protein Eng 1999 12 8 635 638 10.1093/protein/12.8.635 10469823
    • (1999) Protein Eng , vol.12 , Issue.8 , pp. 635-638
    • Zhu, G.P.1    Xu, C.2    Teng, M.K.3    Tao, L.M.4    Zhu, X.Y.5    Wu, C.J.6    Hang, J.7    Niu, L.W.8    Wang, Y.Z.9
  • 32
    • 85024418791 scopus 로고
    • A general principle of increasing protein thermostability
    • 10.2183/pjab.65.146
    • A general principle of increasing protein thermostability. Suzuki Y, Proc Japan Acad Series B-Physl and Bio Sci 1989 65 6 146 148 10.2183/pjab.65.146
    • (1989) Proc Japan Acad Series B-Physl and Bio Sci , vol.65 , Issue.6 , pp. 146-148
    • Suzuki, Y.1
  • 33
    • 0028070908 scopus 로고
    • Crystal structure, at 2.6-A resolution, of the streptomyces lividans xylanase a, a member of the F family of beta-1,4-D-glycanases
    • Crystal structure, at 2.6-A resolution, of the streptomyces lividans xylanase a, a member of the F family of beta-1,4-D-glycanases. Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS, J bio chem 1994 269 33 20811 20814
    • (1994) J Bio Chem , vol.269 , Issue.33 , pp. 20811-20814
    • Derewenda, U.1    Swenson, L.2    Green, R.3    Wei, Y.4    Morosoli, R.5    Shareck, F.6    Kluepfel, D.7    Derewenda, Z.S.8
  • 34
    • 0017455191 scopus 로고
    • The role of the tryptophan-62 residue in the structure and function of lysozyme
    • The role of the tryptophan-62 residue in the structure and function of lysozyme. Churakova NI, Cherkasov IA, Kravchenko NA, Biokhimiia (Moscow, Russia) 1977 42 2 274 276
    • (1977) Biokhimiia (Moscow, Russia) , vol.42 , Issue.2 , pp. 274-276
    • Churakova, N.I.1    Cherkasov, I.A.2    Kravchenko, N.A.3
  • 35
    • 70449707809 scopus 로고    scopus 로고
    • Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase
    • 10.1007/s00792-009-0256-0 19588068
    • Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase. Pennacchio A, Esposito L, Zagari A, Rossi M, Raia CA, Extremophiles 2009 13 5 751 761 10.1007/s00792-009- 0256-0 19588068
    • (2009) Extremophiles , vol.13 , Issue.5 , pp. 751-761
    • Pennacchio, A.1    Esposito, L.2    Zagari, A.3    Rossi, M.4    Raia, C.A.5
  • 37
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • 10.1093/molbev/msr121 21546353
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S, Mol Biol Evol 2011 28 10 2731 2739 10.1093/molbev/msr121 21546353
    • (2011) Mol Biol Evol , vol.28 , Issue.10 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 38
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • 10.1093/nar/gkg520 12824332
    • SWISS-MODEL: an automated protein homology-modeling server. Schwede T, Kopp J, Guex N, Peitsch MC, Nucleic Acids Res 2003 31 13 3381 3385 10.1093/nar/gkg520 12824332
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 39
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • 10.1002/elps.1150181505 9504803
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Guex N, Peitsch MC, Electrophoresis 1997 18 15 2714 2723 10.1002/elps.1150181505 9504803
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 40
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • 10.1093/bioinformatics/bti770 16301204
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Arnold K, Bordoli L, Kopp J, Schwede T, Bioinformatics 2006 22 2 195 201 10.1093/bioinformatics/bti770 16301204
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 41
    • 0035346185 scopus 로고    scopus 로고
    • Swiss-PDB viewer (deep view)
    • 10.1093/bib/2.2.195 11465736
    • Swiss-PDB viewer (deep view). Kaplan W, Littlejohn TG, Brief Bioinform 2001 2 2 195 197 10.1093/bib/2.2.195 11465736
    • (2001) Brief Bioinform , vol.2 , Issue.2 , pp. 195-197
    • Kaplan, W.1    Littlejohn, T.G.2
  • 42
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of ruducing sugar
    • 10.1021/ac60147a030
    • Use of dinitrosalicylic acid reagent for determination of ruducing sugar. Miller GL, Anal Chem 1959 31 3 426 428 10.1021/ac60147a030
    • (1959) Anal Chem , vol.31 , Issue.3 , pp. 426-428
    • Miller, G.L.1


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