The objective of this research is to develop and apply a HILIC UHPLC
stationary phase that allows for separation of intact glycoproteins. In
Chapter 1 I give an overview of the problems of current glycosylation
profiling with regards to biotherapeutics, and my strategy to separate
the intact glycoprotein with HILIC. Chapter 2 describes the methods used
to produce the nonporous packing material and stationary phase. In
Chapter 3 I describe previous work in developing a HILIC polyacrylamide
stationary phase, and further improvements I have made. Chapter 4
describes development of an assay in collaboration with Genentech of
therapeutic mAb glycosylation. In Chapter 5, I show HILIC-MS of digested
ribonuclease B as a beginning step to analyze glycosylated biomarkers.
Identifer | oai:union.ndltd.org:purdue.edu/oai:figshare.com:article/7436645 |
Date | 16 January 2019 |
Creators | Rachel E. Jacobson (5929808) |
Source Sets | Purdue University |
Detected Language | English |
Type | Text, Thesis |
Rights | CC BY 4.0 |
Relation | https://figshare.com/articles/HILIC-MS_analysis_of_protein_glycosylation_using_nonporous_silica/7436645 |
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