Oligomers of l-methionine (Met) and its hydroxy analogue, 2-hydroxy-4-(methylthio)butanoic acid (d,l-HMB) were synthesized with the proteolytic enzyme papain. The Met homooligomers and HMB−Met co-oligomers obtained through the enzymatic reactions were subjected to persulfonation and separated with reverse phase liquid chromatography (RPLC). The separated oligomers were characterized with electrospray ionization-mass spectrometry (ESI-MS). The oligomers were also characterized with matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS). The results showed that co-oligomers were predominantly composed of 4−8 Met residues and one HMB residue. The data also suggest that in the co-oligomers, HMB is attached at the N-terminal end of the oligopeptide chain.
- 2 Hydroxy 4 (Methylthio)butanoic Acid,
- Butyric Acid Derivative,
- Methionine,
- Oligomer,
- Papain,
- Unclassified Drug,
- article,
- Enzyme Mechanism,
- Mass Spectrometry,
- Matrix Assisted Laser Desorption Ionization Time of Flight Mass Spectrometry,
- Peptide Analysis,
- Peptide Synthesis,
- Protein Structure,
- Reversed Phase Liquid Chromatography,
- Chromatography, High Pressure Liquid,
- Mass Spectrometry,
- Methionine,
- Papain,
- HMB,
- Methionine,
- Methionine Hydroxy Analogue,
- MHA,
- Oligopeptides,
- Methionine,
- Oligopeptides
Available at: http://works.bepress.com/daniel-forciniti/13/