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

doi:10.1016/S0021-9673(01)90572-2

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 journal › Article › peer-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 language	English
Pages (from-to)	359-366
Number of pages	8
Journal	Journal of Chromatography A
Volume	319
Issue number	C
DOIs	https://doi.org/10.1016/S0021-9673(01)90572-2
Publication status	Published - 1985
Externally published	Yes

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Organic Chemistry

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10.1016/S0021-9673(01)90572-2

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

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).",

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

note = "Funding Information: This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan.",

year = "1985",

doi = "10.1016/S0021-9673(01)90572-2",

language = "English",

volume = "319",

pages = "359--366",

journal = "Journal of Chromatography A",

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TY - JOUR

T1 - Simple and rapid identification of phosphorylated peptides from bovine brain myelin basic protein by reversed-phase high-performance liquid chromatography

AU - Shoji, S.

AU - Ohnishi, J.

AU - Funakoshi, T.

AU - Kubota, Y.

AU - Fukunaga, K.

AU - Miyamoto, E.

AU - Ueki, H.

N1 - Funding Information: This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan.

PY - 1985

Y1 - 1985

N2 - 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).

AB - 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).

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DO - 10.1016/S0021-9673(01)90572-2

M3 - Article

C2 - 2581982

AN - SCOPUS:0021960060

VL - 319

SP - 359

EP - 366

JO - Journal of Chromatography A

JF - Journal of Chromatography A

SN - 0021-9673

IS - C

ER -

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

Abstract

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