C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry.
Peptides or proteins were hydrolyzed by vapors of 90% pentafluoropropionic acid or heptafluorobutyric acid at 90 degrees C for various time periods. The hydrolyzate mixtures analyzed by both fast-atom-bombardment and electrospray ionization mass spectrometry showed a series of C-terminal successive degradation molecular ions. The degradation reaction may be due to the selective formation of an oxazolone ring at the C-terminal amino acid, followed by hydrolytic removal of the C-terminal amino acid. The major side reactions were cleavages of the peptide bonds at the C side of the internal aspartic acid residue and the N side of serine residue.
Tsugita
A
A
Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Japan.
Takamoto
K
K
Kamo
M
M
Iwadate
H
H
D000595:Amino Acid Sequence; D005466:Fluorocarbons; D005934:Glucagon / Q000737:chemistry; D006868:Hydrolysis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D005466:Fluorocarbons; D010446:Peptide Fragments; C033094:perfluorobutyric acid; C033093:perfluoropropionic acid; D005934:Glucagon