-transparent.png){kind=logo}
A rotatable dual-target probe was used for accurate mass measurement in fast atom bombardment mass spectrometry to determine the structures of unknown amino acid residues or post-translationally modified structures in peptides or proteins. The results obtained in measurement of tryptic peptides (with molecular weights of up to 2000) of the A-subunit of vero-toxin I indicated that the mass values obtained are sufficiently accurate and reproducible to allow the generation of the possible elemental compositions for modifications in peptides. By this method, the structural modifications of the N-terminal of a recombinant human leukocyte interferon A and novel halogenated amino acids in sperm-activating peptides from the egg-jelly of sea urchins were determined.
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
September 1987,
The Journal of biological chemistry,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
December 1989,
Biomedical & environmental mass spectrometry,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
January 1995,
Methods in molecular biology (Clifton, N.J.),
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
January 1996,
Methods in enzymology,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
October 1982,
Science (New York, N.Y.),
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
January 1989,
Journal - Association of Official Analytical Chemists,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
March 1990,
Biomedical & environmental mass spectrometry,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
October 1988,
Biomedical & environmental mass spectrometry,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
May 1994,
Biological mass spectrometry,
T Takao, and
K Yoshino, and
N Suzuki, and
Y Shimonishi
November 1990,
Biomedical & environmental mass spectrometry,
