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Primary sequence confirmation of the β‐amyloid peptide from hereditary cerebral haemorrhage with amyloidosis (Dutch type) by collisional activation of the doubly charged ion
Author(s) -
Orlando R.,
Vassilev V. P.
Publication year - 1992
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200210804
Subject(s) - peptide , protein primary structure , chemistry , peptide sequence , amyloid (mycology) , amyloidosis , sequence (biology) , isoleucine , edman degradation , tandem mass spectrometry , biochemistry , amino acid , mass spectrometry , leucine , gene , pathology , chromatography , medicine , inorganic chemistry
High‐energy collisional activation of doubly charged peptide ions allows direct sequential analysis of peptides over 4 kDa, including leucine‐/isoleucine determinations. This technique was used to verify the sequence of an intact β‐amyloid peptide associated with hereditary cerebral haemorrhage with amyloidosis Dutch type (4.2 kDa), which resists both enzymatic digestion and Edman sequencing. Additionally, this approach shows promise for the primary sequence confirmation of a wide variety of large peptides by tandem mass spectrometry.