Characterization of four GO‐type proteins purified from bovine brain membranes
- 24 April 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 263 (2) , 369-372
- https://doi.org/10.1016/0014-5793(90)81416-l
Abstract
Recently we reported there were at least four types of GO or GO‐like proteins in bovine brain membranes based on their elution profiles from Mono Q columns and their immunological reactivities; one of the proteins was purified as an α‐monomeric form, and the others as αβγ‐trimers. The four proteins, of which α‐subunits were confirmed to be a family of GO‐type by an immunoblot analysis, were thus referred toas αO 1, GO 2, GO 3 and GO 4, respectively, in order of their elutions from the column. Immunostained peptide mappings arising from proteolytic digestions of the four α‐subunits, together with their fragmentation patterns containing radiolabeled ADP‐ribose that had been incorporated by pertussis toxin‐catalyzed ADP‐ribosylation, suggested that the four GO‐α were classified into either of two groups such as α1 and GO 2‐α or GO 3‐α and GO 4‐α. The kinetic parameters of their GTPase activities, however, revealed that there were different properties between αO 1 and GO 2‐α or GO 3‐α and GO 4‐α. Thus, the four GO‐type proteins appeared to be different entities from one another.Keywords
This publication has 16 references indexed in Scilit:
- Purification of GTP‐binding proteins from bovine brain membranesFEBS Letters, 1989
- Purification and characterization of subforms of the guanine‐nucleotide‐binding proteins Gαi and GαoEuropean Journal of Biochemistry, 1989
- GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxinFEBS Letters, 1988
- Purification of heterotrimeric GTP-binding proteins from brain: identification of a novel form of GoBiochemistry, 1988
- Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins).Journal of Biological Chemistry, 1988
- Identification of three pertussis toxin substrates (41, 40 and 39 kDa proteins) in mammalian brain Comparison of predicted amino acid sequences from G‐protein α‐subunit genes and cDNAs with partial amino acid sequences from purified proteinsFEBS Letters, 1988
- 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
- Primary structure of the α-subunit of transducin and its relationship to ras proteinsNature, 1985
- A rapid, sensitive, and specific method for the determination of protein in dilute solutionAnalytical Biochemistry, 1973