Abstract
Various types of amyloid fibril proteins were described but the mechanism of their formation, from “fragments” of Bence-Jones proteins (B.J.), remains unresolved. It is generally accepted that in AL-amyloidosis they represent degradation products of BJ.-proteins rather than independently synthesized polypeptides [1]. Amyloid fibrils are deposited in 6-15% of patients with “Plasma Cell Dyscrasias” (PCD) [2] and in 20 to 25% of patients with “Light Chain disease” [3]. The amino-acid sequences of amyloid fibril polypeptides and of monoclonal proteins, isolated from the serum and/or urine of PCD patients, were determined and found to be structurally closely related [3,4,5]. Certain types of light chains may be more “amyloidogenic” than others and such “amyloidogenic” proteins could be unusually susceptible to proteolysis, due to distinctive segments in their variable regions [6]. We have determined the complete amino-acid sequence of the urinary AL Bence-Jones protein POL and compared its primary structure to that of other B.J. proteins from patients with multiple myeloma with and without amyloidosis.
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© 1991 Springer Science+Business Media Dordrecht
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Pick, A.I., Kratzin, H.D., Barnikol-Watanabe, S., Hilschmann, N. (1991). Complete Amino-Acid Sequence of AL-Bence-Jones Protein POL of the Lambda I Subclass. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_44
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DOI: https://doi.org/10.1007/978-94-011-3284-8_44
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