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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U2 - 10.1016/S0021-9673(01)90572-2
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 -