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J. Biol. Chem., Vol. 265, Issue 22, 12955-12959, Aug, 1990

Beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase. Comparison with the phosphodiesterase family

VM Lipkin, NV Khramtsov, IA Vasilevskaya, NV Atabekova, KG Muradov, VV Gubanov, T Li, JP Johnston, KJ Volpp and ML Applebury
Shemyakin Institute of Bioorganic Chemistry, Union of Soviet Socialist Republics Academy of Sciences, Moscow.

A group of cDNA clones encoding the beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase were isolated for structural analysis. The encoded polypeptide has 853 residues with a calculated molecular mass of 98 kDa. The beta-subunit is 72% identical to the rod cGMP phosphodiesterase alpha-subunit. Like the alpha-subunit and the cone alpha'-subunit, the beta-subunit belongs to the family of phosphodiesterase genes. The beta- and alpha-subunits are more similar to each other than either is to the cone alpha'-subunit, suggesting either that the beta- and alpha-subunits diverged more recently or that their divergence was restrained by the rod functional environment.
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