Determination of methionine sulfoxide content of intact protein based on rearrangement of sulfoxide with acetic anhydride

Lunder, T. L.

doi:10.1016/0003-2697(72)90467-8

Cited by 8 publications

(4 citation statements)

References 15 publications

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“…Partial destruction of MetSO was thus indicated to have occurred during alkaline hydrolysis. Although MetSO has been considered to be stable to alkaline hydrolysis (Neumann, 1972), this stability to alkali has been questioned (Lunder, 1972).…”

Section: Resultsmentioning

confidence: 99%

Specific oxidation of methionine to methionine sulfoxide by dimethyl sulfoxide

Lipton¹,

Bodwell²

1976

J. Agric. Food Chem.

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Section: Resultsmentioning

confidence: 99%

Specific oxidation of methionine to methionine sulfoxide by dimethyl sulfoxide

Lipton¹,

Bodwell²

1976

J. Agric. Food Chem.

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“…An attempt to quantitate methionine oxidation via the Pummerer rearrangement was reported in 1972 by Lunder . However, we have been unable to reproduce his results, and there are no published papers that used this protocol.…”

Section: Resultsmentioning

confidence: 91%

Repurposing the Pummerer Rearrangement: Determination of Methionine Sulfoxides in Peptides

et al. 2019

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The reversible oxidation of methionine residues in proteins has emerged as a biologically important post‐translational modification. However, detection and quantitation of methionine sulfoxide in proteins is difficult. Our aim is to develop a method for specifically derivatizing methionine sulfoxide residues. We report a Pummerer rearrangement of methionine sulfoxide treated sequentially with trimethylsilyl chloride and then 2‐mercaptoimidazole or pyridine‐2‐thiol to produce a dithioacetal product. This derivative is stable to standard mass spectrometry conditions, and its formation identified oxidized methionine residues. The scope and requirements of dithioacetal formation are reported for methionine sulfoxide and model substrates. The reaction intermediates have been investigated by computational techniques and by 13C NMR spectroscopy. These provide evidence for an α‐chlorinated intermediate. The derivatization allows for detection and quantitation of methionine sulfoxide in proteins by mass spectrometry and potentially by immunochemical methods.

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“…interpretation of the results of feeding experiments. Methionine sulfoxide in proteins has been determined by two direct methods, one involving alkaline hydrolysis and determination of the methionine sulfoxide by automatic amino acid analysis (Neumann, 1967) and the other involving a reaction with acetic anhydride and determination of the formaldehyde formed by a color reaction with chromotropic acid (Lunder, 1972).…”

mentioning

confidence: 99%

“…Upon hydrolysis the methionine sulfone is determined by ion-exchange chromatography (Neumann, 1967;Slump and Schreuder, 1973;Sjóberg and Bostrom, 1977). The direct method, involving alkaline hydrolysis, may result in low recoveries of methionine sulfoxide (Neumann, 1967;Lunder, 1972). The indirect method with iodoacetic acid is complicated and time consuming and is 0021-8561Z83/1431-0063$01.50/0 © 1983 American Chemical Society therefore not very suitable for routine analysis.…”

mentioning

confidence: 99%