Biclonal systemic AL-amyloidosis with one glycosylated and one nonglycosylated AL-protein.
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| Abstract |
The amyloid fibril protein AL was isolated from the spleen of a patient with systemic amyloidosis. Size-exclusion chromatography of the solubilized amyloid fibrils revealed a distinct, retarded asymmetric peak. The symmetrical part of the peak showed on SDS-PAGE two positive periodic acid Schiff-staining bands at 14 and 16 kDa. Staining with Coomassie Brilliant Blue revealed in addition two proteins with masses of 13 and 20 kDa. The 14 and 16 kDa bands were the strongest ones. N-Terminal analyses of the four blotted bands showed that the N-termini were the same in all cases. Elucidation of the amino acid sequence established an AL-chain of 157 residues as well as a fragment covering positions 188-207 of the constant region. Two tryptic peptides derived from the same region, positions 25-46, showed an identical sequence, except for position 34 where both alanine and threonine residues occurred. Monosaccharide compositional analysis of the threonine-containing peptide revealed an oligosaccharide in the N-glycosylation site, position 32-34. Mass analysis of the glycopeptide verified the oligosaccharide. The AL-chains belong to the kappa 3a germline gene and verifies that the glycosylated chain is a mutated form. The AL-chains differ from that of the germline in 14 positions. The J-segment is of JkappaIII and is mutated in position 106.
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| Authors | M Karimi, K Sletten, P Westermark |
| Journal | Scandinavian journal of immunology (Scand J Immunol) Vol. 57 Issue 4 Pg. 319-23 (Apr 2003) ISSN: 0300-9475 [Print] England |
| PMID | 12662294 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
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