Advertisement

The Amino Acid Sequence of a Carbohydrate-Containing Immuno-Globulin-Light-Chain-Type Amyloid Fibril Protein (AL)

  • Ole Kristoffer Olstad
  • Knut Sletten
  • Kim Toft
  • Per Westermark
Chapter

Abstract

The amino acid sequence of AL chain So124 was established from N-terminal analyses of the protein itself and on peptides derived after tryptic digestion, digestion with protease V8, digestion with thermolysin and cleavage with BNPS-skatole. The protein was found to consist of 103 amino acid residues and had an oligosaccharide chain linked to an asparagine residue in position 72. The AL chain was most homologous to the variable region of k-type subgroup III.

Keywords

Amyloid Fibril Tryptic Digestion Complete Amino Acid Sequence Immunoglobulin Light Chain High Performance Liquid Chromato 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    G.G. Glenner, Amyloid deposits and Amyloidosis, N.Engl.J.Med. 302:1283 (1980).CrossRefGoogle Scholar
  2. 2.
    G. Husby and K. Sletten, Chemical and clinical classification of amyloidosis 1985, Scand.J.Immunol. 23:253 (1986).CrossRefGoogle Scholar
  3. 3.
    K. Sletten, P. Westermark, P. Pitkanen, N. Thyresson and O.K. Olstad, Amino acid sequences in amyloid proteins of k-III immunoglobulin light-chain origin, Scand.J.Immunol. 18:557 (1983).CrossRefGoogle Scholar
  4. 4.
    H. Tonoike, F. Kametani, A. Hoshi, T. Shinoda and T. Isobe, Primary structure of the variable region of an amyloidogenic Bence Jones protein NIG-77, Biochem.Biophys.Res.Commun. 126:1228 (1985).CrossRefGoogle Scholar
  5. 5.
    K. Sletten, P. Westermark and G. Husby, Structural studies of the variable region of immunoglobulin light-chaintype amyloid fibril proteins, in: “Amyloidosis”, G.G. Glenner, E.F. Osserman, E.P. Benditt, E. Calkins A.S. Cohen and D. Zucker-Franklin, eds., Plenum Press, New York (1986).Google Scholar
  6. 6.
    M. Eulitz, M. Breuer and R.P. Linke, Is the formation of AL-type amyloid promoted by structural peculiarities of immunoglobulin L-chains?, Biol.Chem.Hoppe-Seyler, 368:863 (1987).CrossRefGoogle Scholar
  7. 7.
    K. Sletten, J. Natvig, G. Husby and J. Juul, The complete amino acid sequence of a prototype immunoglobulin-light-chain-type amyloid-fibril protein AR, Biochem.J. 195:561 (1981).Google Scholar
  8. 8.
    B. Frangione, T. Moloshok and A. Solomon, Primary structure of the variable region of a human VI light chain: Bence Jones protein SUT, J.Immunol. 131:2490 (1983).Google Scholar
  9. 9.
    U.K. Laemmli and M. Favre, Maturation of the head of bacteriophage T-4, J.Mol.Biol. 80:575 (1973).CrossRefGoogle Scholar
  10. 10.
    C.H. Bolton, J.R. Clamp and L. Hough, The use of gasliquid chromatography in investigations on glycoproteins, Biochem.J. 96:5c (1965).Google Scholar
  11. 11.
    B.M. Austen and E.L. Smith, Action of Staphylococcal proteinase on peptides of varying chain length and composition, Biochem.Biophys.Res.Commun. 72:411 (1976).CrossRefGoogle Scholar
  12. 12.
    A. Fontana, Modification of tryptophan with BNPS-skatole, Methods Enzymol. 25:419 (1972).CrossRefGoogle Scholar
  13. 13.
    W.C. Mahoney and M.A. Hermodson, Separation of large denatured peptides by reverse phase high performance liquid chromatography, J.Biol.Chem. 261:8442 (1986).Google Scholar
  14. 14.
    J. Devereux, P. Haeberli and O. Smithies, A comprehensive set of sequence analysis programs for the VAX, Nucleic Acids Res. 12:387 (1984).CrossRefGoogle Scholar
  15. 15.
    E.A. Kabat, T.T. Wu, M. Reid-Miller, H.M. Perry and K.S. Gottesman, 1987 Sequences of Proteins of Immunological Interest, U.S. Dept. of Health and Human Services, Public Health Service N.I.H., Bethesda.Google Scholar
  16. 16.
    E. Holm, K. Sletten and G. Husby, Structural studies of a carbohydrate-containing immunoglobulin-λ-light-chain amyloid-fibril protein (AL) of variable subgroup III, Biochem.J. 239:545 (1986).Google Scholar
  17. 17.
    T. Ohkura, T. Isobe, K. Yamashita and A. Kobota, Structures of the carbohydrate moieties of two monoclonal human λ-type immunoglobulin light chains, Biochemistry, 24:503 (1985).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Ole Kristoffer Olstad
    • 1
    • 2
  • Knut Sletten
    • 1
    • 2
  • Kim Toft
    • 1
    • 2
  • Per Westermark
    • 1
    • 2
  1. 1.Department of BiochemistryUniversity of OsloOsloNorway
  2. 2.Institute of PathologyUniversity of UppsalaUppsalaSweden

Personalised recommendations