Cyclic GMP phosphodiesterase from bovine retina Amino acid sequence of the α-subunit and nucleotide sequence of the corresponding cDNA
Autor: | V.V. Gubanov, K.A. Ischenko, Vasily E. Zagranichny, T. M. Shuvaeva, Yu.A. Ovchinnikov, N.V. Khramtsov, K.G. Muradov, Valery M. Lipkin |
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Jazyk: | angličtina |
Předmět: |
Molecular Sequence Data
Biophysics Biology Biochemistry Retina Amino acid sequence Structural Biology 3' 5'-Cyclic-GMP Phosphodiesterases Complementary DNA Genetics Animals Cloning Molecular Peptide Chain Initiation Translational Molecular Biology Peptide sequence chemistry.chemical_classification Cyclic gmp phosphodiesterase Base Sequence Nucleic acid sequence Protein primary structure Cell Biology DNA (Bovine retina) Molecular biology Enzyme chemistry Acetylation Cyclic GMP phosphodiesterase Bovine retina cDNA cloning Cattle Nucleotide sequence |
Zdroj: | FEBS Letters. (1):169-173 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(87)80530-6 |
Popis: | 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. |
Databáze: | OpenAIRE |
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