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Isolation and Characterization of Amyloid‐Related Serum Protein SAA as a Low Molecular Weight Protein
Author(s) -
ANDERS R. F.,
NATVIG J. B.,
MICHAELSEN T. E.,
HUSBY G.
Publication year - 1975
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1975.tb02642.x
Subject(s) - amyloidosis , serum amyloid a , serum amyloid a protein , size exclusion chromatography , immunoprecipitation , amyloid (mycology) , protein subunit , chemistry , biochemistry , molecular mass , microbiology and biotechnology , medicine , biology , immunology , enzyme , gene , inorganic chemistry , inflammation
With direct immunoprecipitation or gel filtration under dissociating conditions, amyloid‐related serum protein SAA has been isolated as a low molecular weight protein from the serum of two patients with rheumatoid arthritis but without known amyloidosis. The isolated protein SAA showed antigenic identity and an amino acid composition that was similar, but not identical, with isolated fibril protein AA., Molecular weight estimations suggest that protein SAA is approximately 50%, larger than protein AA and has a molecular weight of 14,000–15,000 daltons Preliminary results indicate that protein SAA from a patient with amyloidosis has a similar small molecular weight subunit.