Cyclic GMP phosphodiesterase from bovine retina Amino acid sequence of the α-subunit and nucleotide sequence of the corresponding cDNA

The α-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 α-subunit contains 858 amino acid residues, its N-terminal amino group being acetylated. The partial...

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Veröffentlicht in:FEBS letters 1987-10, Vol.223 (1), p.169-173
Hauptverfasser: Ovchinnikov, Yu.A., Gubanov, V.V., Khramtsov, N.V., Ischenko, K.A., Zagranichny, V.E., Muradov, K.G., Shuvaeva, T.M., Lipkin, V.M.
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Sprache:eng
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Zusammenfassung:The α-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 α-subunit contains 858 amino acid residues, its N-terminal amino group being acetylated. The partial primary structure of the enzyme, β-subunit has also been elucidated. A significant homology has been found between the α- and β-subunits of cGMP phosphodiesterase.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)80530-6