Cyclic GMP phosphodiesterase from cattle retina

Ovchinnikov, Yu.A.; Липкин, В. М.; Kumarev, V.P.; Gubanov, V.V.; Khramtsov, N.V.; Akhmedov, Novrouz B.; Gubanov, V.E.; Muradov, Khakim G.

doi:10.1016/0014-5793(86)80830-4

Cited by 132 publications

(63 citation statements)

References 14 publications

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“…The enzyme was isolated, and the 7-subunit was separated from a-and/~-subunits as described in [5]. The mixture of c~-and ~-subunits was hydrolyzed with cyanogen bromide.…”

Section: Methodsmentioning

confidence: 99%

“…Then the peptides were fractionated by gel-filtration and separated by HPLC on Ultrasphere ODS. Their amino acid sequence was established according to [5].…”

Section: Methodsmentioning

confidence: 99%

“…cDNA clone libraries in vector pUC 8 were produced by a poly(A) + fraction of RNA from bovine retina as described in [5]. To initiate synthesis of the first cDNA chain use was made of: (i) oligo(dT)12-18; (ii) specific oligodeoxyribonucleotide probes; (iii) statistic mixture of primers (DNA hydrolysate with an average size of 10-20 nucleotides).…”

Section: Methodsmentioning

confidence: 99%

“…analyzed in parallel to solve the enzyme 7-subunit primary structure [5]. The structure of large subunits was studied similarly.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 1987

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The ct-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 ~t-subunit contains 858 amino acid residues, its N-terminal amino group being acetylated. The partial primary structure of the enzyme fl-subunit has also been elucidated. A significant homology has been found between the ct-and fl-subunits of cGMP phosphodiesterase.

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“…The enzyme was isolated, and the 7-subunit was separated from a-and/~-subunits as described in [5]. The mixture of c~-and ~-subunits was hydrolyzed with cyanogen bromide.…”

Section: Methodsmentioning

confidence: 99%

“…Then the peptides were fractionated by gel-filtration and separated by HPLC on Ultrasphere ODS. Their amino acid sequence was established according to [5].…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…analyzed in parallel to solve the enzyme 7-subunit primary structure [5]. The structure of large subunits was studied similarly.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 1987

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“…For instance, the N-terminus of rod PDEy is reported to be acetylated [22]. Perhaps such a modification is necessary to achieve optimal interactions or protein folding.…”

Section: K Values For the Inhibitory Subunitsmentioning

confidence: 99%

Affinities of bovine photoreceptor cGMP phosphodiesterases for rod and cone inhibitory subunits

et al. 1993

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Rods and cones have analogous phototransduction components and cycles, but differ from each other in their physiological response to light. Differences between the affinities of rod and cone phosphodiesterase (PDE) catalytic subunits for their respective inhibitory subunits could potentially contribute to these physiological differences. To test this idea, we expressed both the 13 kDa PDE subunit, unique to a subset of bovine retinal cones [(1990) J. Biol. Chem. 265, 11259-I 12641, and the rod PDE 11 kDa inhibitory subunit in E. coli, purified them, and compared their abilities to inhibit rod and cone PDE catalytic subunits. Rod PDE has similar K, values (-80 PM) for both the rod and cone recombinant inhibitory subunits. Activated cone PDE has K, values of 200 pM for the cone 13 kDa subunit and 600 pM for rod PDEy.

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Ultrastructural localization of gustducin immunoreactivity in microvilli of type II taste cells in the rat

et al. 2000

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Gustducin is a transducin-like G protein (guanine nucleotide-binding protein) that is expressed in taste bud cells. Gustducin is believed to be involved in bitter and possibly sweet taste transduction. In the present study, we demonstrate that a subset of type II cells displays immunoreactivity to antisera directed against gustducin in taste buds of rat circumvallate papilla. Immunogold particles are present both in the microvilli and cytoplasm of the immunoreactive cells. Quantitative analysis of the data suggests that the number of colloidal gold particles (P<0.001) and nanogold particles (P<0.01) in the immunoreactive type II cells are much greater than in type I cells. There are also approximately 2.5 times (P<0.05) as many colloidal gold particles associated with the microvilli versus the cytoplasm in the immunoreactive type II cells. The ultrastructural distribution of gustducin immunoreactivity is consistent with its proposed role in the initial events of sensory transduction by gustatory receptor cells.

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Cyclic GMP phosphodiesterase from cattle retina

Cited by 132 publications

References 14 publications

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

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

Affinities of bovine photoreceptor cGMP phosphodiesterases for rod and cone inhibitory subunits

Ultrastructural localization of gustducin immunoreactivity in microvilli of type II taste cells in the rat

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