Simple and rapid identification of phosphorylated peptides from bovine brain myelin basic protein by reversed-phase high-performance liquid chromatography

S. Shoji, J. Ohnishi, T. Funakoshi, Y. Kubota, K. Fukunaga, E. Miyamoto, H. Ueki

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

The phosphorylation sites of the myelin basic protein from bovine brain were determined after phosphorylation with a cyclic 3′:5′-phosphate-dependent protein kinase from the same source. Three phosphorylated peptides were selectively rapidly separated, before and after dephosphorylation, by reversed-phase high-performance liquid chromatography on a styrene 250 column under alkaline conditions. Partial sequencing of the peptides by automated Edman degradation revealed that the serine-115 residue located in the main encephalitogenic determinant of the protein was a phosphorylation site, in addition to the two phosphorylation sites established (threonine-34 and serine-55).

Original languageEnglish
Pages (from-to)359-366
Number of pages8
JournalJournal of Chromatography A
Volume319
Issue numberC
DOIs
Publication statusPublished - 1985
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Simple and rapid identification of phosphorylated peptides from bovine brain myelin basic protein by reversed-phase high-performance liquid chromatography'. Together they form a unique fingerprint.

Cite this