Degree
Master of Science
Program
Chemistry
Supervisor
Ken Yeung
Abstract
ADP-ribosylation is one of many biologically important protein post-translational modifications (PTMs) that received considerable research interest in the past decade. The first part of this work presents the analysis of ADP-ribosylation, with special focus on the catalytic domain of an enzyme ARTD-10. The application of capillary electrophoresis (CE) is proposed in this work to separate the in vitro enzymatic mono-ADP-ribosylated ARTD-10 catalytic domain and its unmodified form. Another exciting aspect of CE application with growing interest is the sample preparation. The effectiveness and efficiency for in-vial reaction, in-capillary mixed reaction and on-capillary-tip reaction by performing methyl esterification on phophopeptides were investigated, in the context of sub-microliter (sub-µL) sample handling in an attempt to provide insight into future integration of such in-capillary derivatization with enrichment. In this work, a miniaturized in-capillary methyl esterification derivatization method was developed, allowing the efficient sample handling of sub-µL quantities as a scaled-down sample preparation approach.
Recommended Citation
Huang, Ming, "Analysis of ADP-Ribosylation and Protein Sample Preparation by Capillary Electrophoresis" (2012). Electronic Thesis and Dissertation Repository. 901.
https://ir.lib.uwo.ca/etd/901