Multiple isoforms of ADP-ribosylated G-like proteins from mammalian thyroid membranes.
Bovine, canine, and porcine thyroid membrane proteins which were [32P] ADP-ribosylated by cholera and pertussis toxin in vitro were analyzed by one and two-dimensional polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. These three mammalian species have similar cholera toxin substrates (Mr 42,000 and 48,000) and pertussis toxin substrates (Mr 40,000). Resolution by two dimensional gel electrophoresis of these ribosylated proteins revealed that they each consist of at least 6 distinct polypeptides with similar isoelectric points ranging from approximately 5.5-7.0.
D000246:Adenosine Diphosphate Ribose; D000818:Animals; D002417:Cattle; D002772:Cholera Toxin; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000302:isolation & purification*; D007526:Isoelectric Point; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D037342:Pertussis Toxin; D011110:Polymorphism, Genetic; D013961:Thyroid Gland / Q000378:metabolism*; D010566:Virulence Factors, Bordetella
D008565:Membrane Proteins; D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D002772:Cholera Toxin; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins