NOVEL FRAGMENTATION PROCESS OF PEPTIDES BY COLLISION-INDUCED DECOMPOSITION IN A TANDEM MASS-SPECTROMETER - DIFFERENTIATION OF LEUCINE AND ISOLEUCINE
NOVEL FRAGMENTATION PROCESS OF PEPTIDES BY COLLISION-INDUCED DECOMPOSITION IN A TANDEM MASS-SPECTROMETER - DIFFERENTIATION OF LEUCINE AND ISOLEUCINE
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DOI:
10.1021/ac00148a019
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发表时间:
1987-11-01
影响因子:
7.4
通讯作者:
WATSON, JT
中科院分区:
文献类型:
--
作者:
JOHNSON, RS;MARTIN, SA;WATSON, JT
The mass spectra produced upon collision-induced decomposition of the protonated molecules of peptides often exhibit peaks that correspond to ions that are formed by cleavage of the -N-CR- bond along the peptide chain followed by cleavage of the .beta.,.gamma. bond if R has the general structure -C.beta.-C.gamma.-R''. Ions produced in this manner are assigned the notation Wn and are helpful in the characterization of the amino acid at that position. Most important is the differentiation of the amino acids leucine and isoleucine, which is generally difficult or impossible by mass spectrometry. Aromatic amino acids do not undergo this fragmentation because it would involve cleavage of a C-Ar bond, neither does alanine, which would involve loss of a hydrogen radical, nor does glycine, which lacks a .beta.,.gamma. bond. The nature of this fragmentation process is demonstrated by exact mass measurements and precursor-product ion studies.