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High‐performance liquid chromatographic mass spectrometric examination of C ‐methylation artifacts from the permethylation reaction of peptides
Author(s) -
Yu T. J.,
Karger B. L.,
Vouros Paul
Publication year - 1983
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200101203
Subject(s) - methyl iodide , chemistry , methylation , chromatography , mass spectrometry , glycine , carbanion , amino acid , mass spectrum , high performance liquid chromatography , organic chemistry , biochemistry , gene
Abstract Combined high performance liquid chromatography mass spectrometry using a moving belt interface was used to investigate C ‐methylation artifacts arising from the permethylation reaction of peptides with methyl sulfinyl carbanion and methyl iodide. C ‐Methylation was not limited to glycine but, depending on the reaction conditions, other amino acids were also susceptible to it. In the absence of a glycine residue, preference for C ‐methylation of the C‐terminus amino acid was observed. The use of on‐line high performance liquid chromatography mass spectrometry allowed the separation of N, O, C ‐methylated from the N, O, S ‐permethylated derivatives, thus facilitating interpretation of the mass spectra.