Purification and identification of two pertussis-toxin-sensitive GTP-binding proteins of bovine spleen.
Two alpha subunits of GTP-binding proteins were purified from bovine spleen membranes. Both proteins were ADP-ribosylated by pertussis toxin in the presence of beta gamma subunits. The major protein had a molecular mass of 40 kDa and its immunological reactivity and fragmentation pattern by limited proteolysis were identical with those of the alpha subunit of Gi2. The minor protein had a molecular mass of 41 kDa and its partial amino acid sequences completely matched with those predicted from human and rat Gi3 alpha cDNAs.
Morishita
R
R
Institute for Developmental Research, Aichi Prefectural Colony, Japan.
Asano
T
T
Kato
K
K
Itoh
H
H
Kaziro
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D019204:GTP-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D037342:Pertussis Toxin; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013154:Spleen / Q000378:metabolism*; D010566:Virulence Factors, Bordetella / Q000494:pharmacology*
D046911:Macromolecular Substances; D010566:Virulence Factors, Bordetella; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins