Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/10510
Title: | Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction | Authors: | Schulz, Patricia Cruz, Tony F. Moscarello, Mario A. |
Issue Date: | Oct-1988 | Publisher: | American Chemical Society | Citation: | Biochemistry. 27:20 (1988) 7793-7799 | Abstract: | Fractions containing myelin of varying degrees of compaction were prepared from human white matter. Protein kinase activity in these fractions was measured by using both endogenous and exogenous myelin basic protein (MBP) as substrates. In both cases, less compact myelin fractions possessed higher levels of protein kinase activity than the compact myelin fraction. In addition, the specific activity of phosphorylated basic protein was greater in the loosely compacted fractions than in compact multilamellar myelin. When basic protein in compact myelin or the myelin fractions was phosphorylated by the endogenous kinase, approximately 70% of the [32P]phosphate was incorporated at a single site, identified as Ser-102. The remaining 30% was found in three other minor sites. Electron microscopy of less compact myelin showed it was composed of fewer lamellae which correlated with a relative decrease in the proportion of cationic charge isomers (microheteromers) when MBP was subjected to gel electrophoresis at alkaline pH. The shift in charge microheterogeneity of basic protein to the less cationic isomers in the less compact myelin fractions correlated with an increase in protein kinase activity and a greater specific activity of phosphorylated basic protein. | URI: | https://hdl.handle.net/10316/10510 | ISSN: | 0006-2960 | DOI: | 10.1021/bi00420a031 | Rights: | openAccess |
Appears in Collections: | FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Endogenous Phosphorylation of Basic Protein.pdf | 2.5 MB | Adobe PDF | View/Open |
SCOPUSTM
Citations
21
checked on Oct 14, 2024
WEB OF SCIENCETM
Citations
5
21
checked on Oct 2, 2024
Page view(s)
263
checked on Oct 15, 2024
Download(s) 10
1,373
checked on Oct 15, 2024
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.