Electronic Thesis and Dissertation Repository

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.


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