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J. Biol. Chem., Vol. 263, Issue 17, 8133-8141, Jun, 1988
PG Gillespie and JA Beavo
The biochemical bases for the differences in cone and rod photoreceptor
physiology have not been thoroughly examined because of the difficulty in
obtaining cone photoreceptor components. We report here the purification
and preliminary characterization of a bovine cyclic GMP phosphodiesterase
(PDE) which is enriched in cone photoreceptors. The cone PDE was purified
at least 15,000-fold to apparent homogeneity from bovine retinas by
DEAE-cellulose and cGMP-Sepharose affinity chromatography. The
trypsin-activated cone PDE hydrolyzed cGMP with efficiency similar to that
of the rod PDE. However, a number of characteristics distinguished the cone
PDE from the rod isozyme including the subunit structure. As previously
reported, the apparent molecular weight of the cone PDE large subunit
(alpha') was slightly larger than either of the large subunits of the rod
PDE (93,500 versus 88,000 and 84,000). Three other smaller polypeptides
were associated with the alpha' subunit (Mr = 11,000, 13,000, and 15,000),
one of which (11,000) may be identical to the rod PDE gamma subunit. Cone
phosphodiesterase binds at least 10-fold more cyclic GMP/mol of PDE than
the rod photoreceptor isozyme. Cyclic GMP binds to this noncatalytic site
with high affinity (Kd = 11 nM) and dissociates very slowly (t1/2 = 10-20
min at 37 degrees C). Purified rod transducin activated the cone PDE in
solution to at least 90% of the trypsin- activated level. The concentration
of rod transducin required for half- maximal activation of cone PDE (15 nM)
was 50-fold lower than that necessary for half-maximal activation of rod
PDE. Thus several properties of the cone phosphodiesterase clearly
distinguish it from the rod isozyme and could account for some differences
in cone and rod physiology.
Characterization of a bovine cone photoreceptor phosphodiesterase purified by cyclic GMP-sepharose chromatography
Department of Pharmacology, University of Washington, Seattle 98195.
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