Systemic Amyloidosis: Tissue Specific Variability in the Primary Structure of Amyloid Proteins
Amyloidosis comprises a heterogenous group of diseases, characterized by the deposition of fibrillar proteins in various tissues and organs. Amyloid proteins consist of a number of chemically diverse polypeptides of low molecular weight that share several characteristic tinctorial properties, B-pleated sheet conformation and solubility in low ionic strength solutions, which facilitates their isolation from other tissue constituents (1,2).
KeywordsFamilial Mediterranean Fever Amyloid Fibril Amyloid Protein Free Light Chain Systemic Amyloidosis
Unable to display preview. Download preview PDF.
- 1.Pras, M., Gafni, J., 1977, The nature of amyloid, in:“Immunochemistry: an advanced textbook” L.E. Glynn, M.W. Steward, eds., John Wiley and Sons, Ltd., London, England.Google Scholar
- 9.Pras, M., Prelli, F., Gafni, J., and Frangione B., Genetic heterogeneity of familial amyloid polyneuropathies of Jewish type, in:“Amyloidosis” G.G. Glenner, E.F. Osserman, E.P. Bensitt, E. Calkins, A.S. Cohen, and D. Zucker-Franklin, eds., Plenum Press, New-York.Google Scholar