26 April 2000 Exonuclease reactivity using MALDI-TOF mass spectrometry
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Proceedings Volume 3924, Molecular Imaging: Reporters, Dyes, Markers, and Instrumentation; (2000) https://doi.org/10.1117/12.384247
Event: BiOS 2000 The International Symposium on Biomedical Optics, 2000, San Jose, CA, United States
Abstract
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was used to study, among many of its important activities, the exonuclease activity of exonuclease III (EC 3.1.11.2), a metal-dependent enzyme. The technique is capable of analyzing the mixture of DNA substrates in the reaction. Time dependent measurement of the reaction mixture provided kinetics data of the enzyme. It was found that among divalent metals studied, Mn, which increased the rate of reactions by two orders of magnitude, is the best cofactor for exonuclease III.
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Uraiwan Puapaiboon, Uraiwan Puapaiboon, Jaran Jai-nhuknan, Jaran Jai-nhuknan, James A. Cowan, James A. Cowan, } "Exonuclease reactivity using MALDI-TOF mass spectrometry", Proc. SPIE 3924, Molecular Imaging: Reporters, Dyes, Markers, and Instrumentation, (26 April 2000); doi: 10.1117/12.384247; https://doi.org/10.1117/12.384247
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