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Characterization of four G O ‐type proteins purified from bovine brain membranes
Author(s) -
Inanobe Atsushi,
Shibasaki Hisayuki,
Takahashi Katsunobu,
Kobayashi Ichiro,
Tomita Urara,
Ui Michio,
Katada Toshiaki
Publication year - 1990
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(90)81416-l
Subject(s) - membrane , characterization (materials science) , chemistry , biochemistry , materials science , nanotechnology
Recently we reported there were at least four types of G O or G O ‐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 G O ‐type by an immunoblot analysis, were thus referred toas α O 1 , G O 2 , G O 3 and G O 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 G O ‐α were classified into either of two groups such as α 1 and G O 2 ‐α or G O 3 ‐α and G O 4 ‐α. The kinetic parameters of their GTPase activities, however, revealed that there were different properties between α O 1 and G O 2 ‐α or G O 3 ‐α and G O 4 ‐α. Thus, the four G O ‐type proteins appeared to be different entities from one another.