Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of the alpha-subunit and nucleotide sequence of the corresponding cDNA.
The alpha-subunit primary structure of cyclic GMP phosphodiesterase has been determined by parallel analysis of the protein amino acid sequence and the corresponding cDNA nucleotide sequence. The enzyme alpha-subunit contains 858 amino acid residues, its N-terminal amino group being acetylated. The partial primary structure of the enzyme beta-subunit has also been elucidated. A significant homology has been found between the alpha- and beta-subunits of cGMP phosphodiesterase.
Ovchinnikov YuA
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
Gubanov
V V
VV
Khramtsov
N V
NV
Ischenko
K A
KA
Zagranichny
V E
VE
Muradov
K G
KG
Shuvaeva
T M
TM
Lipkin
V M
VM
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D008969:Molecular Sequence Data; D010442:Peptide Chain Initiation, Translational; D012160:Retina / Q000201:enzymology*
D004247:DNA; D015106:3',5'-Cyclic-GMP Phosphodiesterases