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Primary structure of the α‐subunit of bovine adenylate cyclase‐inhibiting G‐protein deduced from the cDNA sequence
Author(s) -
Nukada Toshihide,
Tanabe Tsutomu,
Takahashi Hideo,
Noda Masaharu,
Haga Kazuko,
Haga Tatsuya,
Ichiyama Arata,
Kangawa Kenji,
Hiranaga Masuyo,
Matsuo Hisayuki,
Numa Shosaku
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80347-7
Subject(s) - adenylate kinase , cyclase , protein primary structure , complementary dna , protein subunit , transducin , nucleic acid sequence , microbiology and biotechnology , peptide sequence , g protein , biology , biochemistry , messenger rna , homology (biology) , chemistry , amino acid , dna , gene , enzyme , receptor
The primary structure of the α‐subunit of the adenylate cyclase‐inhibiting G‐protein (g i ) has been deduced from the nucleotide sequence of cloned DNA complementary to the bovine cerebral mRNA encoding the polypeptide. A much higher degree of amino acid sequence homology is observed between the α‐subunits of G i and transducin (68%) than between those of G i and the adenylate cyclase‐stimulating G‐protein (G s ) (43%) or between those of transucin and G s (42%).