The amino acid sequence of a glycosylated AL-chain from a patient with primary amyloidosis.

An amyloid fibril protein (Owe) related to primary amyloidosis was found to be a glycosylated complete immunoglobulin light chain (AL). The amino acid sequence revealed a protein composed of 214 residues and with a glycosylation site in position 20. The sequence established an AL V-region corresponding to a kappa 1b germline gene, but differs from that in 12 positions.

Serum amyloid P component in mink, a non-glycosylated protein with affinity for phosphorylethanolamine and phosphorylcholine.

Experimental AA amyloidosis in the mink is used as a model for the amyloid disease process. In that context it is important to characterize the different proteins involved in the amyloid formation. In the present work, we have characterized the serum amyloid P component (SAP) in mink.