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Advances in gas chromatographic mass spectrometric protein sequencing. 1—optimization of the derivatization chemistry
Author(s) -
Carr Steven A.,
Herlihy Walter C.,
Biemann K.
Publication year - 1981
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.1200080203
Subject(s) - derivatization , chemistry , chromatography , mass spectrometry , trimethylsilyl , yield (engineering) , bacteriorhodopsin , amino acid , gas chromatography , oligopeptide , peptide , isobutane , organic chemistry , membrane , biochemistry , catalysis , materials science , metallurgy
The derivatization chemistry for conversion of mixtures of oligopeptides to the corresponding N ‐α, (ω)‐trifluoroethyl‐ O ‐trimethylsilyl polyamino alcohols, the derivatives of choice for the sequencing of polypeptides by gas chromatographic mass spectrometry, has been optimized. The improvements have minimized undesirable side reactions and resulted in a five‐ to tenfold increase in sensitivity over previous methods employing either lithium aluminum deuteride or hexadeuterodiborane as the reducing agent. For derivatives of certain very polar peptides increases in yield have exceeded 100‐fold. The procedure has been evaluated with mixtures of synthetic oligopeptides and used in the course of the determination of the amino acid sequence of the membrane protein bacteriorhodopsin, as well as other proteins.