-transparent.png){kind=logo}
Ozone oxidation converted the single, invariant, tryptophan residue to N2-formylkynurenine in alpha-bungarotoxin and cobrotoxin. Upon this modification, the lethal toxicity was significantly reduced in cobrotoxin but mostly retained in alpha-bungarotoxin. Each neurotoxin containing kynurenine instead of tryptophan retained the same antigenicity as the native toxin. Fluorescence and CD spectroscopy revealed that, although the environment and state of the kynurenine residue were similar, [Kyn29]cobrotoxin was much more sensitive to pH change than alpha-[Kyn28]bungarotoxin. In terms of lethal toxicity and conformational stability, the invariant tryptophan residue appears to play a more important role in cobrotoxin, imparting a higher lethal toxicity than that in alpha-bungarotoxin, which has a disulfide bond at Cys29-Cys33.
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
March 1993,
Biochemistry and molecular biology international,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
January 1985,
Biochemical and biophysical research communications,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
October 1982,
International journal of peptide and protein research,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
December 1973,
Biochimica et biophysica acta,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
February 1969,
Journal of biochemistry,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
October 1951,
Experientia,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
October 1980,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
March 2007,
Biochemistry,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
September 1965,
Journal of biochemistry,
C C Chang, and
Y Kawata, and
F Sakiyama, and
K Hayashi
July 1979,
FEBS letters,
