AI Article Synopsis
- Researchers synthesized oligomers from l-methionine (Met) and its analogue, d,l-HMB, using the enzyme papain.
- The resulting oligomers were separated via reverse phase liquid chromatography (RPLC) and characterized using electrospray ionization-mass spectrometry (ESI-MS) and matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS).
- Findings indicated that the co-oligomers mainly consisted of 4-8 Met residues with one HMB residue, and HMB was positioned at the N-terminal end of the oligopeptide chain.
Article Abstract
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.
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| http://dx.doi.org/10.1021/jf026093g | DOI Listing |
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