Abstract
Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.
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- Anders R. F., Natvig J. B., Michaelsen T. E., Husby G. Isolation and characterization of amyloid-related serum protein SAA as a low molecular weight protein. Scand J Immunol. 1975;4(4):397–401. doi: 10.1111/j.1365-3083.1975.tb02642.x. [DOI] [PubMed] [Google Scholar]
- Anders R. F., Natvig J. B., Sletten K., Husby G., Nordstoga K. Amyloid-related serum protein SAA from three animal species: comparison with human SAA. J Immunol. 1977 Jan;118(1):229–234. [PubMed] [Google Scholar]
- Bausserman L. L., Herbert P. N., McAdam K. P. Heterogeneity of human serum amyloid A proteins. J Exp Med. 1980 Sep 1;152(3):641–656. doi: 10.1084/jem.152.3.641. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Benditt E. P., Eriksen N. Amyloid protein SAA is associated with high density lipoprotein from human serum. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4025–4028. doi: 10.1073/pnas.74.9.4025. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Benditt E. P., Eriksen N., Hanson R. H. Amyloid protein SAA is an apoprotein of mouse plasma high density lipoprotein. Proc Natl Acad Sci U S A. 1979 Aug;76(8):4092–4096. doi: 10.1073/pnas.76.8.4092. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Costa P. P., Figueira A. S., Bravo F. R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4499–4503. doi: 10.1073/pnas.75.9.4499. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Franklin E. C. Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin. J Exp Med. 1976 Dec 1;144(6):1679–1682. doi: 10.1084/jem.144.6.1679. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GRABAR P., WILLIAMS C. A. Méthode permettant l'étude conjuguée des proprietés électrophorétiques et immunochimiques d'un mélange de protéines; application au sérum sanguin. Biochim Biophys Acta. 1953 Jan;10(1):193–194. doi: 10.1016/0006-3002(53)90233-9. [DOI] [PubMed] [Google Scholar]
- Glenner G. G. Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N Engl J Med. 1980 Jun 5;302(23):1283–1292. doi: 10.1056/NEJM198006053022305. [DOI] [PubMed] [Google Scholar]
- Gorevic P. D., Levo Y., Chatpar P. C., Frangione B., Franklin E. C. Some effects of the administration of endotoxin in mice. Specific cleavage of serum albumin by an acid protease and the generation of amyloid serum component. J Clin Invest. 1979 Feb;63(2):254–261. doi: 10.1172/JCI109297. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hijmans W., Sipe J. D. Levels of the serum amyloid A protein (SAA) in normal persons of different age groups. Clin Exp Immunol. 1979 Jan;35(1):96–100. [PMC free article] [PubMed] [Google Scholar]
- Husby G. A chemical classification of amyloid. Correlation with different clinical types of amyloidosis. Scand J Rheumatol. 1980;9(1):60–64. doi: 10.1080/03009748009098131. [DOI] [PubMed] [Google Scholar]
- Husby G., Natvig J. B. A serum component related to nonimmunoglobulin amyloid protein AS, a possible precursor of the fibrils. J Clin Invest. 1974 Apr;53(4):1054–1061. doi: 10.1172/JCI107642. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lavie G., Zucker-Franklin D., Franklin E. C. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med. 1978 Oct 1;148(4):1020–1031. doi: 10.1084/jem.148.4.1020. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lavie G., Zucker-Franklin D., Franklin E. C. Elastase-type proteases on the surface of human blood monocytes: possible role in amyloid formation. J Immunol. 1980 Jul;125(1):175–180. [PubMed] [Google Scholar]
- Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenthal C. J., Franklin E. C., Frangione B., Greenspan J. Isolation and partial characterization of SAA-an amyloid-related protein from human serum. J Immunol. 1976 May;116(5):1415–1418. [PubMed] [Google Scholar]
- Rosenthal C. J., Franklin E. C. Serum amyloid A (SAA) protein-interaction with itself and serum albumin. J Immunol. 1977 Aug;119(2):630–634. [PubMed] [Google Scholar]
- Skogen B., Børresen A. L., Natvig J. B., Berg K., Michaelsen T. E. High-density lipoprotein as carrier for amyloid-related protein SAA in rabbit serum. Scand J Immunol. 1979;10(1):39–45. doi: 10.1111/j.1365-3083.1979.tb01332.x. [DOI] [PubMed] [Google Scholar]
- 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]