J. Biol. Chem., Vol. 255, Issue 21, 10199-10204, 11, 1980
Studies on the tryptophan-dependent light emission by prostaglandin hydroperoxidase reaction
T Yoshimoto, S Yamamoto, K Sugioka, M Nakano, C Takyu, A Yamagishi and H Inaba
The chemiluminescence earlier observed upon the incubation of arachidonic
acid with prostaglandin-synthesizing microsomes of sheep vesicular gland
(Marnett et al. (1974) Biochem. Biophys. Res. Commun. 60, 1286-1294) was
reinvestigated with prostaglandin endoperoxide synthetase purified from
bovine vesicular gland microsomes. When the purified enzyme was incubated
with arachidonic acid in the presence of hematin and tryptophan, a rapid
light emission was observed. The fatty acid cyclo-oxygenase activity as
demonstrated with manganese protoporphyrin was not responsible for the
luminescence. When the hematin-requiring prostaglandin hydroperoxidase
reaction (the conversion of prostaglandin G2 to H2) was carried out with
tryptophan, skatole, or 3-indolepropionic acid, the light emission was
observed, but not with either epinephrine or guaiacol in place of
tryptophan. The light intensity was dependent on the concentration of
enzyme, hematin, tryptophan, and prostaglandin G2. Various other
hydroperoxides in addition to prostaglandin G2 were also active. The
luminescence spectrum recorded by a spectrometer equipped with a filter
spectral analyzer gave emission peaks around 500, 550, and 610 nm. The
spectrum was distinguishable from that of singlet oxygen, and was similar
to that reported for a photochemical reaction of tryptophan.
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