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Proceedings Paper

Exonuclease reactivity using MALDI-TOF mass spectrometry
Author(s): Uraiwan Puapaiboon; Jaran Jai-nhuknan; James A. Cowan
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Paper 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.

Paper Details

Date Published: 26 April 2000
PDF: 5 pages
Proc. SPIE 3924, Molecular Imaging: Reporters, Dyes, Markers, and Instrumentation, (26 April 2000); doi: 10.1117/12.384247
Show Author Affiliations
Uraiwan Puapaiboon, The Ohio State Univ. (United States)
Jaran Jai-nhuknan, Bruker Daltonics, Inc. (United States)
James A. Cowan, The Ohio State Univ. (United States)


Published in SPIE Proceedings Vol. 3924:
Molecular Imaging: Reporters, Dyes, Markers, and Instrumentation
Darryl J. Bornhop; Kai Licha, Editor(s)

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