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Volumn 411, Issue 1, 2011, Pages 94-99

A high-throughput matrix-assisted laser desorption/ionization-time-of- flight mass spectrometry-based assay of chitinase activity

Author keywords

Chitinase; Enzyme assay; MALDI TOF; Mass spectrometry; Oligosaccharides

Indexed keywords

C (PROGRAMMING LANGUAGE); DESORPTION; DRUG PRODUCTS; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; OLIGOSACCHARIDES; SUBSTRATES;

EID: 79951575820     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.12.027     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0344110241 scopus 로고    scopus 로고
    • Insect chitinases: Molecular biology and potential use as biopesticides
    • DOI 10.1016/S0965-1748(97)00078-7, PII S0965174897000787
    • K.J. Kramer, and S. Muthukrishnan Insect chitinases: molecular biology and potential use as biopesticides Insect Biochem. Mol. 27 1997 887 900 (Pubitemid 28093029)
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , Issue.11 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 2
    • 0027348936 scopus 로고
    • Chitin synthesis and degradation as targets for pesticide action
    • E. Cohen Chitin synthesis and degradation as targets for pesticide action Arch. Insect Biochem. 22 1993 245 261
    • (1993) Arch. Insect Biochem. , vol.22 , pp. 245-261
    • Cohen, E.1
  • 4
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • A. Schlumbaum, F. Mauch, U. Vögeli, and T. Boller Plant chitinases are potent inhibitors of fungal growth Nature 324 1986 365 367
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 5
    • 33748541288 scopus 로고    scopus 로고
    • The Biology of the Gaucher Cell: The Cradle of Human Chitinases
    • DOI 10.1016/S0074-7696(06)52001-7, PII S0074769606520017, A Survey of Cell Biology
    • A.P. Bussink, M. van Eijk, G.H. Renkema, J.M. Aerts, and R.G. Boot The biology of the Gaucher cell: the cradle of human chitinases Intl. Rev. Cytol. 252 2006 71 128 (Pubitemid 44375087)
    • (2006) International Review of Cytology , vol.252 , pp. 71-128
    • Bussink, A.P.1    Van Eijk, M.2    Renkema, G.H.3    Aerts, J.M.4    Boot, R.G.5
  • 6
    • 2942668626 scopus 로고    scopus 로고
    • Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation
    • DOI 10.1126/science.1095336
    • Z. Zhu, T. Zheng, R.J. Homer, Y.-K. Kim, N.Y. Chen, L. Cohn, Q. Hamid, and J.A. Elias Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation Science 304 2004 1678 1682 (Pubitemid 38765861)
    • (2004) Science , vol.304 , Issue.5677 , pp. 1678-1682
    • Zhu, Z.1    Zheng, T.2    Homer, R.J.3    Kim, Y.-K.4    Chen, N.Y.5    Cohn, L.6    Hamid, Q.7    Elias, J.A.8
  • 7
    • 37049008281 scopus 로고    scopus 로고
    • Direct detection of underivatized chitooligosaccharides produced through chitinase action using capillary zone electrophoresis
    • DOI 10.1016/j.ab.2007.08.042, PII S0003269707006999
    • L. Blanes, R.M. Saito, F.A. Genta, J. Donegá, W.R. Terra, C. Ferreira, and C.L. do Lago Direct detection of underivatized chitooligosaccharides produced through chitinase action using capillary zone electrophoresis Anal. Biochem. 373 2008 99 103 (Pubitemid 50014085)
    • (2008) Analytical Biochemistry , vol.373 , Issue.1 , pp. 99-103
    • Blanes, L.1    Saito, R.M.2    Genta, F.A.3    Donega, J.4    Terra, W.R.5    Ferreira, C.6    Do Lago, C.L.7
  • 9
    • 33847421735 scopus 로고    scopus 로고
    • Natural substrate assay for chitinases using high-performance liquid chromatography: A comparison with existing assays
    • DOI 10.1016/j.ab.2006.12.044, PII S0003269707000036
    • I.-M. Krokeide, B. Synstad, S. Gseidnes, S.J. Horn, V.G.H. Eijsink, and M. Sørlie Natural substrate assay for chitinases using high-performance liquid chromatography: a comparison with existing assays Anal. Biochem. 363 2007 128 134 (Pubitemid 46348973)
    • (2007) Analytical Biochemistry , vol.363 , Issue.1 , pp. 128-134
    • Krokeide, I.-M.1    Synstad, B.2    Gaseidnes, S.3    Horn, S.J.4    Eijsink, V.G.H.5    Sorlie, M.6
  • 11
    • 0026506381 scopus 로고
    • A rapid and sensitive microassay for determination of chitinolytic activity
    • K.J. McCreath, and G.W. Gooday A rapid and sensitive microassay for determination of chitinolytic activity J. Microbiol. Methods 4 1992 229 237
    • (1992) J. Microbiol. Methods , vol.4 , pp. 229-237
    • McCreath, K.J.1    Gooday, G.W.2
  • 13
    • 0017610344 scopus 로고    scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • J. Molano, A. Duran, and E. Cabib A rapid and sensitive assay for chitinase using tritiated chitin Anal. Biochem. 83 1997 648 656
    • (1997) Anal. Biochem. , vol.83 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 14
    • 0026640655 scopus 로고
    • Antifungal proteins from plants: Purification, molecular cloning, and antifungal properties of chitinases from maize seed
    • Q.K. Huynh, C.M. Hironaka, E.B. Levine, C.E. Smith, J.R. Borgmeyer, and D.M. Shah Antifungal proteins from plants: purification, molecular cloning, and antifungal properties of chitinases from maize seed J. Biol. Chem. 267 1992 6635 6640
    • (1992) J. Biol. Chem. , vol.267 , pp. 6635-6640
    • Huynh, Q.K.1    Hironaka, C.M.2    Levine, E.B.3    Smith, C.E.4    Borgmeyer, J.R.5    Shah, D.M.6
  • 15
    • 79953269003 scopus 로고    scopus 로고
    • Modification of recombinant maize ChitA chitinase by fungal chitinase-modifying proteins
    • T.A. Naumann, Modification of recombinant maize ChitA chitinase by fungal chitinase-modifying proteins, Mol. Plant Pathol., in press, doi:10.1111/j.1364-3703.2010.00677.x.
    • Mol. Plant Pathol
    • Naumann, T.A.1
  • 16
    • 77950377779 scopus 로고    scopus 로고
    • Functionalized C-glycoside ketohydrazones: Carbohydrate derivatives that retain the ring integrity of the terminal reducing sugar
    • N.P.J. Price, M.J. Bowman, S.L. Gall, M.A. Berhow, D.F. Kendra, and P. Lerouge Functionalized C-glycoside ketohydrazones: carbohydrate derivatives that retain the ring integrity of the terminal reducing sugar Anal. Chem. 82 2010 2893 2899
    • (2010) Anal. Chem. , vol.82 , pp. 2893-2899
    • Price, N.P.J.1    Bowman, M.J.2    Gall, S.L.3    Berhow, M.A.4    Kendra, D.F.5    Lerouge, P.6
  • 17
    • 33750045148 scopus 로고    scopus 로고
    • Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes
    • DOI 10.1111/j.1742-4658.2006.05487.x
    • I.A. Hoell, B. Dalhus, E.B. Heggset, S.I. Aspmo, and V.G.H. Eijsink Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes FEBS J. 273 2006 4889 4900 (Pubitemid 44583513)
    • (2006) FEBS Journal , vol.273 , Issue.21 , pp. 4889-4900
    • Hoell, I.A.1    Dalhus, B.2    Heggset, E.B.3    Aspmo, S.I.4    Eijsink, V.G.H.5
  • 18
    • 0029876802 scopus 로고    scopus 로고
    • Plant chitinases use two different hydrolytic mechanisms
    • DOI 10.1016/0014-5793(96)00174-3
    • B. Iseli, S. Armand, T. Boller, J.-M. Neuhaus, and B. Henrissat Plant chitinases use two different hydrolytic mechanisms FEBS Lett. 382 1996 186 188 (Pubitemid 26092252)
    • (1996) FEBS Letters , vol.382 , Issue.1-2 , pp. 186-188
    • Iseli, B.1    Armand, S.2    Boller, T.3    Neuhaus, J.-M.4    Henrissat, B.5
  • 19
    • 0023110718 scopus 로고
    • Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitor
    • S. Sakuda, A. Isogai, S. Matsumoto, and A. Suzuki Search for microbial insect growth regulators: II. Allosamidin, a novel insect chitinase inhibitor J. Antibiot. 40 1987 296 300 (Pubitemid 17044876)
    • (1987) Journal of Antibiotics , vol.40 , Issue.3 , pp. 296-300
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4
  • 22
    • 41149127141 scopus 로고    scopus 로고
    • TMG-chitotriomycin, an enzyme inhibitor specific for insect and fungal β-N-acetylglucosaminidases, produced by actinomycete Streptomyces anulatus NBRC 13369
    • DOI 10.1021/ja077641f
    • H. Usuki, T. Nitoda, M. Ichikawa, N. Yamaji, T. Iwashita, H. Komura, and H. Kanzaki TMG-chitotriomycin, an enzyme inhibitor specific for insect and fungal β-N-acetylglucosaminidases produced by actinomycete Streptomyces anulatus NBRC 13369 J. Am. Chem. Soc. 130 2008 4146 4152 (Pubitemid 351429886)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.12 , pp. 4146-4152
    • Usuki, H.1    Nitoda, T.2    Ichikawa, M.3    Yamaji, N.4    Iwashita, T.5    Komura, H.6    Kanzaki, H.7
  • 23
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, an N-acetyl-β-hexosaminidase inhibitor that implicates acetamido participation
    • DOI 10.1021/ja960826u
    • S. Knapp, D. Vocadlo, Z. Gao, B. Kirk, J. Lou, and S.G. Withers NAG-thiazoline, an N-acetyl-β-hexosaminidase inhibitor that implicates acetamido participation J. Am. Chem. Soc. 118 1996 6804 6805 (Pubitemid 26248188)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.28 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.2    Gao, Z.3    Kirk, B.4    Lou, J.5    Withers, S.G.6
  • 24
    • 24944469869 scopus 로고    scopus 로고
    • Synthesis and kinetic analysis of the N-acetylhexosaminidase inhibitor XylNAc-isofagomine
    • DOI 10.1021/jo051117e
    • S. Knapp, C. Yang, S. Pabbaraja, B. Rempel, S. Reid, and S.G. Withers Synthesis and kinetic analysis of the N-acetylhexosaminidase inhibitor XylNAc-isofagomine J. Org. Chem. 70 2005 7715 7720 (Pubitemid 41318534)
    • (2005) Journal of Organic Chemistry , vol.70 , Issue.19 , pp. 7715-7720
    • Knapp, S.1    Yang, C.2    Pabbaraja, S.3    Rempel, B.4    Reid, S.5    Withers, S.G.6
  • 25
    • 77952865632 scopus 로고    scopus 로고
    • Development of GlcNAc-inspired iminocyclitiols as potent and selective N-acetyl-β-hexosaminidase inhibitors
    • C.-W. Ho, S.D. Popat, T.-W. Liu, K.-C. Tsai, M.-J. Ho, W.-H. Chen, A.-S. Yang, and C.-H. Lin Development of GlcNAc-inspired iminocyclitiols as potent and selective N-acetyl-β-hexosaminidase inhibitors ACS Chem. Biol. 5 2010 489 497
    • (2010) ACS Chem. Biol. , vol.5 , pp. 489-497
    • Ho, C.-W.1    Popat, S.D.2    Liu, T.-W.3    Tsai, K.-C.4    Ho, M.-J.5    Chen, W.-H.6    Yang, A.-S.7    Lin, C.-H.8
  • 27
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 resolution
    • P.J. Hart, H.D. Pfluger, A.F. Monzingo, T. Hollis, and J.D. Robertus The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 resolution J. Mol. Biol. 248 1995 402 413
    • (1995) J. Mol. Biol. , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 28
    • 77955778566 scopus 로고    scopus 로고
    • Structure of full-length class i chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering
    • Y. Kezuka, M. Kojima, R. Mizuno, K. Suzuki, T. Watanabe, and T. Nonaka Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering Proteins 78 2010 2295 2305
    • (2010) Proteins , vol.78 , pp. 2295-2305
    • Kezuka, Y.1    Kojima, M.2    Mizuno, R.3    Suzuki, K.4    Watanabe, T.5    Nonaka, T.6
  • 33
    • 0037938666 scopus 로고    scopus 로고
    • Family 19 chitinase from rice (Oryza sativa L.): Substrate-binding subsites demonstrated by kinetic and molecular modeling studies
    • DOI 10.1023/A:1023972007681
    • C. Sasaki, Y. Itoh, H. Takehara, S. Kuhara, and T. Fukamizo Family 19 chitinase from rice (Oryza sativa L.): substrate-binding subsites demonstrated by kinetic and molecular modeling studies Plant Mol. Biol. 52 2003 43 52 (Pubitemid 36708404)
    • (2003) Plant Molecular Biology , vol.52 , Issue.1 , pp. 43-52
    • Sasaki, C.1    Itoh, Y.2    Takehara, H.3    Kuhara, S.4    Fukamizo, T.5
  • 35
    • 34248545259 scopus 로고    scopus 로고
    • Mass spectrometry for enzyme assays and inhibitor screening: An emerging application in pharmaceutical research
    • DOI 10.1002/mas.20127
    • K.D. Greis Mass spectrometry for enzyme assays and inhibitor screening: an emerging application in pharmaceutical research Mass Spectrom. Rev. 26 2007 324 339 (Pubitemid 46750373)
    • (2007) Mass Spectrometry Reviews , vol.26 , Issue.3 , pp. 324-339
    • Greis, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.