Multiple GTP-binding proteins from cholinergic synaptic vesicles.
Cholinergic synaptic vesicles purified from the electric organ of the marine ray, Discopyge ommata, contain 2 different size classes of GTP-binding proteins: one or more with an apparent molecular weight (MW) between 37 and 41 kDa, and 3 major and at least 2 minor proteins with MW between 20 and 29 kDa. These GTP-binding proteins were detectable using the alpha 32P-GTP overlay technique and covalent modification with bacterial toxins. The higher MW GTP-binding proteins are ADP-ribosylated by pertussis toxin and 2 of the lower MW GTP-binding proteins are sensitive to botulinum toxin.
Ngsee
J K
JK
Department of Biological Sciences, Stanford University, California 94305.
Miller
K
K
Wendland
B
B
Scheller
R H
RH
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000818:Animals; D001905:Botulinum Toxins / Q000494:pharmacology; D002845:Chromatography; D005399:Fishes; D019204:GTP-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D010275:Parasympathetic Nervous System / Q000378:metabolism* / Q000648:ultrastructure; D037342:Pertussis Toxin; D013572:Synaptic Vesicles / Q000378:metabolism*; D010566:Virulence Factors, Bordetella / Q000494:pharmacology
D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D037342:Pertussis Toxin; D001905:Botulinum Toxins; D019204:GTP-Binding Proteins