title: Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D006801:Humans; D007381:Intermediate Filament Proteins / Q000032:analysis*; D008970:Molecular Weight; D016900:Neurofilament Proteins; D010766:Phosphorylation; D013045:Species Specificity; D013552:Swine
chemical_list: D007381:Intermediate Filament Proteins; D016900:Neurofilament Proteins