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Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of the alpha-subunit and nucleotide sequence of the corresponding cDNA.
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
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.
PMID: 2822478 [PubMed - indexed for MEDLINE]
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Cited by 15 PubMed Central articles
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Identification and characterization of DdPDE3, a cGMP-selective phosphodiesterase from Dictyostelium.
Kuwayama H, Snippe H, Derks M, Roelofs J, Van Haastert PJ.
Biochem J. 2001 Feb 1; 353(Pt 3):635-44.
[Biochem J. 2001]
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Rod photoreceptor cGMP-phosphodiesterase: analysis of alpha and beta subunits expressed in human kidney cells.
Piriev NI, Yamashita C, Samuel G, Farber DB.
Proc Natl Acad Sci U S A. 1993 Oct 15; 90(20):9340-4.
[Proc Natl Acad Sci U S A. 1993]
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Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases.
Clarke S, Vogel JP, Deschenes RJ, Stock J.
Proc Natl Acad Sci U S A. 1988 Jul; 85(13):4643-7.
[Proc Natl Acad Sci U S A. 1988]
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