Prealbumin in Swedish Patients with Senile Systemic Amyloidosis and Familial Amyloidotic Polyneuropathy

• Published in: Scandinavian Journal of Immunology
• Main Authors: FELDING, P., FEX, G., WESTERMARK, P., OLOFSSON, B. O., PITKÄNEN, P., BENSON, L.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1985
• Subjects: Northern Sweden
• Online Access: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01412.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-3083.1985.tb01412.x; https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-3083.1985.tb01412.x

A prealbumin (PA)‐like protein was demonstrated in amyloid fibrils both from a patient with senile systemic amyloidosis (SSA) and from a patient in northern Sweden with familial amyloidotic polyneuropathy (FAP). The investigated properties of this protein were similar in the two types of fibrils. The protein had molecular weight, antigenic determinants, and at least one eysteinyl residue in common with the subunit of normal PA. In contrast to normal PA. it contained disulphide‐linked subunits and was to some extent bound to the fibril via the eysteinyl residues. The noncovalent forces between its subunits were weaker than in normal PA. It constituted part of the previously described AScl protein of the SSA fibrils. Proteins with lower molecular weight than the PA monomer were major proteins in both SSA and FAP fibrils. These proteins had similar properties in the two kinds of fibril and may be derived from PA. PA in serum from Swedish patients with FAP and SSA was normal with regard to the isoclectric pH of the monomers and tetramers.