Primary structure of the α‐subunit of bovine adenylate cyclase‐inhibiting G‐protein deduced from the cDNA sequence
Первичная структура α-субъединицы ингибирующего аденилатциклазу G-белка крупного рогатого скота, выведенная на основании последовательности кДНК
1986-03-03
SCID: 54.1/bbbwwkaw
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Gi alpha-subunitadenylate cyclase-inhibiting G-proteinamino acid sequence homologybovine cerebral mRNAcDNA sequence
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Abstract (AI)
The primary structure of the alpha-subunit of the adenylate cyclase-inhibiting G-protein (Gi) 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 alpha-subunits of Gi and transducin (68%) than between those of Gi and the adenylate cyclase-stimulating G-protein (Gs) (43%) or between those of transducin and Gs (42%).
Key Findings
1
Gi and transducin α-subunits show 68% amino acid sequence homology.
2
Gi shares substantially greater sequence homology with transducin than with the stimulatory Gs α-subunit (43%).
3
The primary amino acid sequence of the bovine Gi protein α-subunit was deduced from the nucleotide sequence of cloned cDNA derived from bovine brain mRNA.
4
Transducin and Gs α-subunits exhibit 42% amino acid sequence homology, indicating greater divergence between these proteins than between Gi and transducin.
Research Object
The alpha-subunit of the bovine adenylate cyclase-inhibiting G-protein (Gi)
Research Subject
Its deduced primary amino acid structure and sequence homology with the alpha-subunits of transducin and the adenylate cyclase-stimulating G-protein (Gs)
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1986-03-03
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