Primary structure of bovine cerebellum GTP-binding protein G39and its effect on the adenylate cyclase system
- 21 December 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 226 (1) , 91-95
- https://doi.org/10.1016/0014-5793(87)80557-4
Abstract
The primary structure of bovine cerebellum GTP-binding protein α-subunit, protein G39 was determined by parallel analysis of the protein amino acid sequence and the corresponding cDNA nucleotide sequence. The protein consists of 354 amino acid residues and has a molecular mass of 40064 Da. High homology between G39 and other G-proteins, especially rat brain Go was shown. An assumption is made that certain brain adenylate cyclase system properties are determined by the presence of G39Keywords
This publication has 14 references indexed in Scilit:
- Deduced amino acid sequence of bovine retinal Go alpha: similarities to other guanine nucleotide-binding proteins.Proceedings of the National Academy of Sciences, 1987
- The GTP-binding protein, Go9 regulates neuronal calcium channelsNature, 1987
- Cyclic GMP phosphodiesterase from cattle retinaFEBS Letters, 1986
- Go, a guanine nucleotide-binding protein: immunohistochemical localization in rat brain resembles distribution of second messenger systems.Proceedings of the National Academy of Sciences, 1986
- Molecular cloning and sequence determination of cDNAs for alpha subunits of the guanine nucleotide-binding proteins Gs, Gi, and Go from rat brain.Proceedings of the National Academy of Sciences, 1986
- Primary structure of the α‐subunit of bovine adenylate cyclase‐inhibiting G‐protein deduced from the cDNA sequenceFEBS Letters, 1986
- Deduced primary structure of the alpha subunit of the GTP-binding stimulatory protein of adenylate cyclase.Proceedings of the National Academy of Sciences, 1986
- Primary structure of the α‐subunit of bovine adenylate cyclase‐stimulating G‐protein deduced from the cDNA sequenceFEBS Letters, 1986
- G proteins and dual control of adenylate cyclaseCell, 1984
- A new method for sequencing DNA.Proceedings of the National Academy of Sciences, 1977