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Facile assignment of sequence ions of a peptide labelled with 18 O at the carboxyl terminus
Author(s) -
Takao Toshifumi,
Hori Hideaki,
Okamoto Kazutake,
Harada Akira,
Kamachi Mikiharu,
Shimonishi Yasutsugu,
Matsuo Takckiyo
Publication year - 1991
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290050703
Subject(s) - chemistry , n terminus , peptide , peptide sequence , c terminus , sequence (biology) , ion , dissociation (chemistry) , mass spectrometry , fast atom bombardment , amino acid , stereochemistry , biochemistry , chromatography , organic chemistry , gene
The combination of collision‐induced dissociation (CID) and linked‐scan analysis was used for analysing the sequence ions from the precursor ion of a peptide, which had been labelled with 18 O at its carboxyl terminus (C‐terminus) using 40 atom % H 2 18 O. The CID and linked‐scan mass spectrum of the labelled peptide gave two series of sequence‐ion signals: the one, originating from the C‐terminus of the labelled peptide, showed a doublet signal due to the part‐incorporation of 18 O into the carboxyl group at the C‐terminus, while the other, originating from the amino terminus (N‐terminus), has the natural isotopic ion distribution. From the distribution of the isotopic ions in a single CID spectrum, the sequence ions containing the C‐terminus could be readily differentiated from those containing the N‐terminus, allowing the facile assignment of sequence ions to the amino‐acid sequence of peptide by CID and linked‐scan analysis. This method was successfully applied to determination of the amino‐acid sequence of the light‐chain of mouse anti‐porphyrin monoclonal antibody.