Exonuclease reactivity using MALDI-TOF mass spectrometry

Uraiwan Puapaiboon; Jaran Jai-nhuknan; James A. Cowan

doi:10.1117/12.384247

26 April 2000 Exonuclease reactivity using MALDI-TOF mass spectrometry

Uraiwan Puapaiboon, Jaran Jai-nhuknan, James A. Cowan

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.

Citation Download Citation

Uraiwan Puapaiboon, Jaran Jai-nhuknan, and James A. Cowan "Exonuclease reactivity using MALDI-TOF mass spectrometry", Proc. SPIE 3924, Molecular Imaging: Reporters, Dyes, Markers, and Instrumentation, (26 April 2000); https://doi.org/10.1117/12.384247

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available