ADP-ribosylation of myelin basic proteins isolated from normal and mutant mouse brains.
Myelin basic proteins (MBPs) have been shown to be ADP-ribosylated in-vitro by cholera toxin in the presence of NAD. Since acid-soluble extracts of brain contain other proteins in the 14-32 kD range (such as histones) in addition to MBP's, the identification of the ADP-ribosylated proteins was uncertain. To determine that only the MBP's were ADP-ribosylated, the acid-soluble fractions from several murine mutants were prepared. Thus, in the Shiverer mutants, none of the proteins in the 14-32 kD range were ADP-ribosylated; in the Myelin-deficient mutant, some of ADP-ribosylation was observed but none in the Jimpy mutant, consistent with our demonstration that the least cationic isomer cannot be ADP-ribosylated.
Boulias
C
C
Hospital for Sick Children, Department of Biochemistry, Toronto, Ontario, Canada.
Moscarello
M A
MA
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001345:Autoradiography; D001923:Brain Chemistry / Q000187:drug effects*; D002384:Catalysis; D002772:Cholera Toxin / Q000494:pharmacology; D066298:In Vitro Techniques; D051379:Mice; D008816:Mice, Jimpy; D008818:Mice, Neurologic Mutants; D004676:Myelin Basic Protein / Q000235:genetics / Q000378:metabolism*
D004676:Myelin Basic Protein; D000246:Adenosine Diphosphate Ribose; D002772:Cholera Toxin