Abstract
Prostate-specific antigen (PSA) is a single-chain glycoprotein that is used as a biomarker for prostate-related diseases. PSA has one known posttranslational modification, a sialylated diantennary N-linked oligosaccharide attached to the asparagine residue N45. In this study capillary electrophoresis (CE) was employed to separate the isoforms of seven commercially available free PSA samples, two of which were specialized: enzymatically active PSA and noncomplexing PSA. The free PSA samples examined migrated as four to nine distinct, highly resolved peaks, indicating the presence of several isoforms differing in their oligosaccharide compositions. Overall, the use of CE provides a rapid, reproducible method for separation of PSA into its individual isoforms.
Original language | English (US) |
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Pages (from-to) | 318-327 |
Number of pages | 10 |
Journal | Analytical Biochemistry |
Volume | 339 |
Issue number | 2 |
DOIs | |
State | Published - Apr 15 2005 |
Externally published | Yes |
Bibliographical note
Funding Information:MJD thanks the National Science Foundation for the Chemometrics Fellowship and the National Institute of Standards and Technology for their support of this research.
Keywords
- Capillary electrophoresis
- Heterogeneity
- Isoforms
- Prostate-specific antigen