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 |
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Hauptverfasser: | , , , , , , , |
Format: | Artikel |
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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(87)80530-6 |