ADP-ribosyltransferase activity in myelin membranes isolated from human brain |
| |
Authors: | Chris Boulias Fabrizio G Mastronardi Mario A Moscarello |
| |
Institution: | (1) Division of Biochemistry Research, The Hospital for Sick Children, 555 University Avenue, M5G 1X8 Toronto, Ontario, Canada |
| |
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 GTPS and was specific for the -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.Abbreviations ADP-ribose
adenosine diphosphate ribose
- APAD
3-acetylpyridine adenine dinucleotide
- ATP
adenosine triphosphate
- C-1, 2, 3 etc
MBP components isolated by CM52 chromatography
- EDTA
ethylenediaminetetraacetic acid
- GTP
guanosine triphosphate
- GTPS
guanosine 5-(3-0-thio)triphosphate
- INH
isonicotinic acid hydrazide
- MBP
myelin basic protein
- NAD
nicotinamide adenine dinucleotide
- PMSF
phenylmethylsulfonyl fluoride
- PLP
proteolipid protein
Special issue dedicated to Dr. Leon S. Wolfe. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|