Amino acid sequences of tryptic peptides of (A) amyloid fibril protein isolated from postmortem kidney of patient II-10, and (B) plasma κ light-chain from a member of the next generation (III-15) with biopsy-proven amyloidosis. The normal sequence of the constant region of κ light-chains is shown. Residue numbering is by Kabat et al.8 The lines indicate the sequences obtained by Edman degradation of HPLC-purified tryptic peptides. The parentheses at the ends of the amyloid fibril protein peptides (A) denote residues not completely verified because of decreasingly low Edman degradation yields. The X at residues 131 and 134 denote that no amino acid was identified at these positions. The dots at the ends of some plasma light-chain peptides (B) indicate that the peptide continued but was not analyzed further.
