Journal article
Active sites of the cyclic GMP phosphodiesterase γ-subunit of retinal rod outer segments
FEBS letters, Vol.234(2), pp.287-290
1988
DOI: 10.1016/0014-5793(88)80100-5
PMID: 2455657
Abstract
Monoclonal antibodies were prepared to the γ-subunit of the cGMP phosphodiesterase. One of them γp-1, suppresses the activation of phosphodiesterase through the α-subunit of transducin. The γ-subunit fragment 24–45 rich in Arg and Lys residues is involved in γp-1 binding and is essential for the γ-subunit interaction with transducin. Carboxypeptidase Y cleaves off seven amino acid residues from the C-terminus of the γ-subunit resulting in phosphodiesterase activation. Thus, the C-terminal fragment of γ-subunit participates in phosphodiesterase inhibition.
Details
- Title: Subtitle
- Active sites of the cyclic GMP phosphodiesterase γ-subunit of retinal rod outer segments
- Creators
- V.M Lipkin - Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, ul. Miklukho-Maklaya, 16/10, 117871 GSP Moscow V-437 USSRI.L Dumler - Sechenov Institute of Evolutionary Physiology and Biochemistry, USSR Academy of Sciences, prosp. Moresa Toreza, 44, 194223 Leningrad, USSRK.G Muradov - Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, ul. Miklukho-Maklaya, 16/10, 117871 GSP Moscow V-437 USSRN.O Artemyev - Sechenov Institute of Evolutionary Physiology and Biochemistry, USSR Academy of Sciences, prosp. Moresa Toreza, 44, 194223 Leningrad, USSRR.N Etingof - Sechenov Institute of Evolutionary Physiology and Biochemistry, USSR Academy of Sciences, prosp. Moresa Toreza, 44, 194223 Leningrad, USSR
- Resource Type
- Journal article
- Publication Details
- FEBS letters, Vol.234(2), pp.287-290
- Publisher
- Elsevier B.V
- DOI
- 10.1016/0014-5793(88)80100-5
- PMID
- 2455657
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Language
- English
- Date published
- 1988
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
- Record Identifier
- 9984025412102771
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