Abstract
AL proteins, six of the k-type and ten of the λ-type, were isolated from amyloid fibrils obtained from amyloid-laden organs of patients with plasma cell dyscrasias. The AL proteins were subgroups in VkI, VkIII, VλI, VλII, VλIII, VλIV and VλVI. The molecular weight ranged from 12 to 22 kD. At least 4 of the k-type and 5 of the λ-type AL proteins contained carbohydrate. Elucidation of the primary structure of three AL-chains sub-grouped in VλI, VλII and VλIII, revealed several positions where some unique amino acid interchanges had occurred. A comparison of AL-chains and Bence Jones proteins from patients without amyloidosis, indicated that the homology between two AL-chains of the same subgroup was less than that between an AL-chain and a Bence Jones protein. Location of oligosaccharide chains were established by amino acid sequence analyses of glycopeptides. The glycosylation sites were located in the CDR 1, CDR 3 and the FR 4.
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© 1986 Plenum Press, New York
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Sletten, K., Westermark, P., Husby, G. (1986). Structural Studies of the Variable Region of Immunoglobulin Light-Chain-Type Amyloid Fibril Proteins. In: Glenner, G.G., Osserman, E.F., Benditt, E.P., Calkins, E., Cohen, A.S., Zucker-Franklin, D. (eds) Amyloidosis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2199-6_59
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DOI: https://doi.org/10.1007/978-1-4613-2199-6_59
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