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J. Biol. Chem., Vol. 255, Issue 23, 11619-11624, Dec, 1980
A Yamazaki, I Sen, MW Bitensky, JE Casnellie and P Greengard
Two classes of high affinity, cGMP-specific binding sites have been found
in association with a peripheral membrane protein in rod outer segments.
[3H]cGMP and a photoaffinity label, 8-N3-[32P]cIMP, have been used to study
these cGMP binding sites. The cGMP binding sites co- migrated with rod
outer segment phosphodiesterase (EC 3.1.4.17) upon Bio-Gel A-0.5m column
chromatography, sucrose density gradient centrifugation, and isoelectric
focusing (pI 5.35). Upon sodium dodecyl sulfate-polyacrylamide gel
electrophoresis, the 8-N3-[32P]cIMP-labeled protein also migrated in a
position identical with that of purified phosphodiesterase. Scatchard
analysis, using purified phosphodiesterase, revealed the presence of two
classes of cGMP binding sites with apparent KD values of 0.16 and 0.83
microM. A number of observations indicated that these high affinity,
cGMP-specific binding sites are distinct from the phosphodiesterase
catalytic site. cAMP, which is a substrate for phosphodiesterase, did not
bind to the high affinity cGMP specific sites. Limited tryptic proteolysis
of phosphodiesterase resulted in a striking activation of the catalytic
activity and a 96% loss of cGMP binding. 1-Methyl-3-isobutylxanthine
inhibited phosphodiesterase activity and enhanced the specific binding of
cGMP. Mg2+ was necessary for phosphodiesterase activity, but not for high
affinity cGMP binding. Finally, phosphodiesterase activity and the
cGMP-specific high affinity sites showed different stabilities on storage
in phosphate buffer. These specific high affinity cGMP binding sites may be
involved in the regulation of phosphodiesterase activity.
Cyclic GMP-specific, high affinity, noncatalytic binding sites on light- activated phosphodiesterase
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