Determination of amino acid sequences in peptides by mass spectrometry. Desulfurization of sulfur-containing peptides
| Autor: | J.E.G. Barnett, Edgar Lederer, B.C. Das, E. Sach, Raoul Toubiana |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
chemistry.chemical_classification
Methionine Protein mass spectrometry Stereochemistry Chemistry Sulfonium Biophysics Peptide Cell Biology Biochemistry Amino acid Residue (chemistry) chemistry.chemical_compound Structural Biology Genetics Organic chemistry Bottom-up proteomics Molecular Biology Cysteine |
| Zdroj: | FEBS Letters. 8:207-209 |
| ISSN: | 0014-5793 |
| Popis: | The mass spectrometric technique for the sequence determination of amino acids in peptides has received a new impetus since procedures for 0, N-permethylation of peptide derivatives have been described [ 1, 2; for a review, see ref. 3] . However, difficulties were encountered in applying the permethylation technique to peptides comprising basic amino acids (arginine, histidine, etc.) as well as sulfur-containing amino acids (methionine, cystine, cysteine, etc.) since during methylation (using methyl iodide) quaternary ammonium or sulfonium salts of low volatility are formed rendering them unsuitable for mass spectrometric analysis. Methionine peptides are also reported [4] to give undesirable by-products during methylation with Ag20, CH,I. The problem of an arginine residue in a peptide could be solved [S] by its conversion to an ornithine residue on treatment with hydrazine [6] prior to N-acetylation and permethylation. To overcome the difficulties with histidinecontaining peptides, the cleavage of the imidazole ring by exhaustive treatment with diethyl pyrocarbonate, before applying the methylation procedure, has recently been suggested [7] . For sulfur-containing peptides, it became obvious that the formation of sulfonium salts could be avoided |
| Databáze: | OpenAIRE |
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