Primary structure of bovine cerebellum GTP‐binding protein G39 and its effect on the adenylate cyclase system

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 homo...

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Bibliographic Details
Published in:FEBS letters 1987-12, Vol.226 (1), p.91-95
Main Authors: Ovchinnikov, Yu.A., Slepak, V.Z., Pronin, A.N., Shlensky, A.B., Levina, N.B., Voeikov, V.L., Lipkin, V.M.
Format: Article
Language:English
Subjects:
Adenylate cyclase
Adenylyl Cyclases - metabolism
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Base Sequence
Binding and carrier proteins
Biological and medical sciences
Bovine cerebellum
Cattle
cDNA cloning
Cerebellum - metabolism
DNA - analysis
Fundamental and applied biological sciences. Psychology
GTP-binding protein
GTP-Binding Proteins - genetics
GTP-Binding Proteins - metabolism
Molecular Sequence Data
Molecular Weight
Nucleotide sequence
Proteins
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Summary: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 G39.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)80557-4