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. 1974 Mar 1;139(3):773–778. doi: 10.1084/jem.139.3.773

NEW, THIRD CLASS OF AMYLOID FIBRIL PROTEIN

G Husby 1, J B Natvig 1, K Sletten 1
PMCID: PMC2139555  PMID: 4204730

Abstract

An unusual protein AR was isolated from the amyloid fibril preparation derived from a patient with primary amyloidosis. Protein AR was unique in its antigenicity, and revealed no structural identity with any known amyloid proteins or with immunoglobulin chains or fragments. Thus a new third class of amyloid fibril proteins besides the immunoglobulin light-chain variable region fragments and the nonimmunoglobulin protein AS, has been characterized. A component antigenically related to protein AR was found in the serum of the patient.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benditt E. P., Eriksen N., Hermodson M. A., Ericsson L. H. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971 Dec 1;19(2):169–173. doi: 10.1016/0014-5793(71)80506-9. [DOI] [PubMed] [Google Scholar]
  2. Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
  3. Husby G., Natvig J. B., Michaelsen T. E., Sletten K., Höst H. Unique amyloid protein subunit common to different types of amyloid fibril. Nature. 1973 Aug 10;244(5415):362–364. doi: 10.1038/244362a0. [DOI] [PubMed] [Google Scholar]
  4. Husby G., Sletten K., Michaelsen T. E., Natvig J. B. Amyloid fibril protein subunit, "protein AS": distribution in tissue and serum in different clinical types of amyloidosis including that associated with myelomatosis and Waldenström's macroglobulinamia. Scand J Immunol. 1973;2(4):395–404. doi: 10.1111/j.1365-3083.1973.tb02048.x. [DOI] [PubMed] [Google Scholar]
  5. Husby G., Sletten K., Michaelsen T. E., Natvig J. B. Antigenic and chemical characterization of non-immunoglobulin amyloid proteins. Scand J Immunol. 1972;1(4):393–400. doi: 10.1111/j.1365-3083.1972.tb03305.x. [DOI] [PubMed] [Google Scholar]
  6. Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973 Aug 1;138(2):373–380. doi: 10.1084/jem.138.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E. C. The characterization of soluble amyloid prepared in water. J Clin Invest. 1968 Apr;47(4):924–933. doi: 10.1172/JCI105784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Putnam F. W., Whitley E. J., Jr, Paul C., Davidson J. N. Amino acid sequence of a kappa Bence Jones protein from a case of primary amyloidosis. Biochemistry. 1973 Sep 11;12(19):3763–3780. doi: 10.1021/bi00743a028. [DOI] [PubMed] [Google Scholar]
  9. Sletten K., Husby G. The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis. Eur J Biochem. 1974 Jan 3;41(1):117–125. doi: 10.1111/j.1432-1033.1974.tb03251.x. [DOI] [PubMed] [Google Scholar]

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