Enzymatic Synthesis and Characterization of L-Methionine and 2-Hydroxy-4-(methylthio)butanoic Acid (HMB) Co-oligomers

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.

Department(s)

Chemistry

Second Department

Chemical and Biochemical Engineering

Keywords and Phrases

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

International Standard Serial Number (ISSN)

0021-8561

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2003 American Chemical Society (ACS), All rights reserved.

Publication Date

01 Apr 2003

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