Author index to volume 220

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.     

Author index to volume 200

Biochemical and partial sequence data reveal the two-domain structure of p36. A loose structure of some 30 residues at the amino-terminus contains the phosphorylatable tyrosine and the binding site for the p11 regulatory chain. The following p33 domain retains the lipid-binding site as well as the Ca2+ site which influences the spectral properties of the single tryptophan and one tyrosine. The combined sequence data covering about 25% of the molecule identify p36 as a unique polypeptide.     

Author index to volume 190

The noted loss of alpha-actinin from the Z-line of myofibrils during post-mortem autolysis, probably following the action of calcium-activated protease, has previously been attributed to its release without degradation. This report shows that in isolated myofibrils alpha-actinin is proteolysed in a Ca2+-sensitive manner presumably via the action of calcium-activated protease.