title: ADP-ribosyltransferase activity in myelin membranes isolated from human brain.
abstract: An ADP-ribosyltransferase has been identified in compact myelin and in several white matter fractions which contain less compact myelin, fractionated on the basis of increasing protein/lipid ratios. One fraction the P3A contained the greatest activity although the activity in compact myelin was only slightly less. The ADP-ribosyltransferase activity of solubilized myelin was stimulated by increasing amounts of GTP gamma S and was specific for the beta-isomer of NAD. Although ADP-ribosylation was demonstrated with the heterotrimeric G proteins in the 40-50 kDa range, the substrate for the ADP-ribosyltransferase in the 20 kDa range was identified as MBP. ADP-ribosyltransferase; myelin basic protein; signal transduction.
authors.affiliation: Division of Biochemistry Research, Hospital for Sick Children, Toronto, Ontario, Canada.
authors.forename: C
authors.initials: C
authors.lastname: Boulias
authors.forename: F G
authors.initials: FG
authors.lastname: Mastronardi
authors.forename: M A
authors.initials: MA
authors.lastname: Moscarello
mesh_terms: D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D005591:Chemical Fractionation; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D006801:Humans; D004676:Myelin Basic Protein / Q000737:chemistry; D009186:Myelin Sheath / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000187:drug effects / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004676:Myelin Basic Protein; D009243:NAD; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D011065:Poly(ADP-ribose) Polymerases