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Direct Evidence for SAA Deposition in Tissues During Murine Amyloidogenesis
Author(s) -
YAKAR S.,
KAPLAN B.,
LIVNEH A.,
MARTIN B.,
MIURA K.,
ALIKHAN Z.,
SHTRASBURG S.,
PRAS M.
Publication year - 1994
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.1365-3083.1994.tb03519.x
Subject(s) - serum amyloid a , amyloidosis , chemistry , amyloid (mycology) , blot , antibody , amino acid , spleen , microbiology and biotechnology , biochemistry , amyloid disease , amyloid fibril , amyloid β , biology , pathology , immunology , medicine , disease , inorganic chemistry , gene , inflammation
To study the mechanism of amyloid deposition, the nature of amyloid proteins formed in experimental murine amyloidosis, was examined. Spleen specimens, 15–60mg, were homogenized and extracted using aqueous acidic acetonitrile, in a recently developed procedure, making it possible to obtain amyloid proteins from minute amounts of tissue. The extracted material, 1.5–4mg, was analysed by Western blotting and ELISA using antibodies recognizing differentially proteins AA and SAA. Two immunoreactive proteins of 8 and 12 KDa were isolated and subjected to amino acid analysis and N‐terminal sequence determination. The results of immunochemical and chemical examination showed that the 8 and 12 KDa proteins represented proteins AA and SAA, respectively. The data obtained provide new direct evidence for SAA deposition in tissues during murine amyloidogenesis.