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Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H
Author(s) -
Geisler Norbert,
Vandekerckhove Joel,
Weber Klaus
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80964-x
Subject(s) - neurofilament , phosphorylation , dephosphorylation , serine , protein subunit , microbiology and biotechnology , biochemistry , biology , chemistry , gene , phosphatase , immunohistochemistry , immunology
Diagonal fingerprinting allows the specific purification of those tryptic peptides which change electrophoretic mobility due to a dephosphorylation step introduced after the first dimension. Nine tryptic peptides from the tail domain of porcine neurofilament M protein identify a minimum of 6 phosphorylated serines. Unexpectedly, four of the nine peptides characterize a region of degenerate repetitive sequences. Results on neurofilament H tail, although less complete, yield longer sequences of degenerate repetitive character. Here, all serines present appear to be contained in a lysine‐serine‐proline unit. This motif also occurs in some but not all M peptides. We suggest that degenerate repetitive sequences in neurofilament M and H tails have a high species‐specific drift.