References
- Husby G, Sletten K. Editorial Review. Chemical and clinical classification of Amyloidosis, 1985. Scand J Immunol 1986; 23: 253–265
- Glenner G G. a). Amyloid deposits and amyloidosis. N Engl Med 1980; 302: 1283–1292
- Glenner G G. b). Amyloid deposits and amyloidosis. N Engl Med 1980; 302: 1333–1343
- Husby G, Sletten K. The structure of amyloid proteins. Amyloidosis, G G Glenner, P P Costa, F de Freitas. Amsterdam Excerpta Medica. 1980; 266–273
- Sletten K, Natvig J B, Husby G, Juul J. The complete amino acid sequence of a prototype immunoglobulin-lambda-light-chain-type amyloid-fibril protein AR. Biochem J 1981; 195: 561–572
- Sletten K, Westermark P, Husby G. Structural studies of the variable region of immunoglobulin light-chain type amyloid fibril proteins. Amyloidosis, G G Glenner, E F Osserman, E P Benditt, E Calkins, A S Cohen, D Zucker-Franklin. Plenum Press, New York 1986; 436–475
- Pras M, Schubert M, Zucker-Franklin D, Rimon A, Franklin E C. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924–933
- Laemmli U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970; 227: 680–685
- Husby G, Sletten K. The complete amino acid sequence of non immunoglobulin amyloid fibril protein AS in rheumatoid arthritis. Eur J Biochem 1974; 41: 117–125
- Fontana A. Modification of tryptophan with BNPS-skatole. Methods Enzymol 1972; 25: 419–442
- Allen G. Sequencing of Proteins and Peptides. Elsevier, North Holland 1981; 58–59
- Chambers R E, Clamp J R. An assessment of methanololysis and other factors used in the analysis of carbohydrate-containing materials. Biochem J 1971; 125: 1009–1018
- Kabat E A, Wu T U, Reid-Miller M, Perry H M, Gottesman K S. Sequences of Protein of Immunological Interest. U. S. Department of Health and Human Services, Washington 1987
- Schacter H. Glycoproteins: Their structure, biosynthesis, and possible clinical implications. Clin Biochem 1984; 17: 3–13
- Toft K G, Sletten K, Husby G. The amino acid sequence of the variable region of a carbohydrate containing immunoglobulin light-chain type amyloid fibril protein. Biol Chem, Hoppe-Seyler 1985; 366: 617–625
- Tveteraas T, Sletten K, Westermark P. The amino acid sequence of a carbohydrate-containing immunoglobulin light-chain type amyloid- fibril protein. Biochem J 1985; 232: 183–190
- Holm E, Sletten S, Husby G. Structural studies of a carbohydrate-containing immunoglobulin-lambda-light-chain amyloid-fibril protein (AL) of variable subgroup III. Biochem J 1986; 239: 545–551
- Liepnieks J J, Benson M D, Dwulet F E. Comparison of the amino acid sequences of ten kappa I amyloid proteins for amyloidogenic sequences. Amyloid and Amyloidosis, J B Natvig, O Forre, G Husby, A Husebekk, B Skogen, K Sletten, P Westermark. Kluwer, Academic Publishers, Dordrecht 1990; 53–156
- Liepnieks J J, Dwulet F E, Benson M D. Amino acid sequence of a kappa I primary (AL) amyloid protein (END). Molecular Immunology 1990; 6: 481–485
- Hurle M R, Helms L R, Li L, Chan W, Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci, USA 1994; 91: 5446–5450