An endogenous inhibitor of the ADP-ribosylation of GTP-binding proteins by pertussis toxin is present in bovine brain.
The ADP-ribosylation of GTP-binding proteins (G-proteins) catalyzed by pertussis toxin was inhibited by endogenous inhibitor activity in the membrane extract of bovine brain. Most of the activity appeared in the fractions eluted from a DEAE-Sephacel column by 0.5 M NaCl. The activity was heat-stable and sensitive to pronase K. The results suggest the presence of an endogenous inhibitor of pertussis toxin in bovine brain.
Hara-Yokoyama
M
M
Department of Physiology, Nihon University School of Dentistry at Matsudo, Chiba, Japan.
Furuyama
S
S
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001923:Brain Chemistry; D002384:Catalysis; D002417:Cattle; D002845:Chromatography; D004355:Drug Stability; D005615:Freezing; D019204:GTP-Binding Proteins / Q000378:metabolism*; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D006358:Hot Temperature; D037342:Pertussis Toxin; D013873:Thionucleotides / Q000378:metabolism; D010566:Virulence Factors, Bordetella / Q000037:antagonists & inhibitors*
D013873:Thionucleotides; D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins