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Volumn 373, Issue 2, 2008, Pages 380-382

Determination of active enzyme concentration using activity-based probes and direct mass spectrometric readout

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MASS SPECTROMETRY; PROBES; TITRATION; ULTRAVIOLET SPECTROSCOPY;

EID: 37549042755     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.11.003     Document Type: Article
Times cited : (7)

References (14)
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    • Evans, M.J.1    Cravatt, B.F.2
  • 6
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    • Activity-based protein profiling: The serine hydrolases
    • Liu Y., Patricelli M.P., and Cravatt B.F. Activity-based protein profiling: The serine hydrolases. Proc. Natl. Acad. Sci. USA 96 (1999) 14694-14699
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 8
    • 24144438205 scopus 로고    scopus 로고
    • A liquid chromatography/mass spectrometry-based method for the selection of ATP competitive kinase inhibitors
    • Khandekar S.S., Feng B., Yi T., Chen S., Laping N., and Bramson N. A liquid chromatography/mass spectrometry-based method for the selection of ATP competitive kinase inhibitors. J. Biomol. Screen. 10 (2005) 447-455
    • (2005) J. Biomol. Screen. , vol.10 , pp. 447-455
    • Khandekar, S.S.1    Feng, B.2    Yi, T.3    Chen, S.4    Laping, N.5    Bramson, N.6
  • 9
    • 33750570678 scopus 로고    scopus 로고
    • A rapid and direct method for the determination of active site accessibility in proteins based on ESI-MS and active site titrations
    • O'Farrell N., Kreiner M., Moore B.D., and Parker M.C. A rapid and direct method for the determination of active site accessibility in proteins based on ESI-MS and active site titrations. Biotechnol. Bioeng. 95 (2006) 767-771
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 767-771
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  • 10
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    • J. M. Daniel, Soft ionization mass spectrometry of biomolecules: A dissertation on ESI and AP-MALDI mass spectrometry, PhD thesis, ETH Zurich, 2005.
  • 11
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    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • Peschke M., Verkerk U.H., and Kebarle P. Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method. J. Am. Soc. Mass Spectrom. 15 (2004) 1424-1434
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1424-1434
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 13
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger K.E., and Reetz M.T. Microbial lipases form versatile tools for biotechnology. Trends Biotechnol. 16 (1998) 396-403
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    • Jaeger, K.E.1    Reetz, M.T.2
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    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • Zhang N., Suen W.C., Windsor W., Xiao L., Madison V., and Zaks A. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng. 16 (2003) 599-605
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.