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An Experimental Model in Mink for Studying the Relation Between Amyloid Fibril Protein AA and the Related Serum Protein, SAA
Author(s) -
HUSBY G.,
NATVIG J. B.,
SLETTEN K.,
NORDSTOGA K.,
ANDERS R. F.
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.tb02690.x
Subject(s) - mink , amyloidosis , guanidine , serum amyloid p component , amyloid (mycology) , chemistry , dithiothreitol , biochemistry , amino acid , biology , medicine , immunology , enzyme , c reactive protein , inflammation , inorganic chemistry , ecology
Experimental amyloidosis was induced in mink by repeated injections with endotoxin. Amyloid fibrils extracted from liver and spleen were fractionated by gel filtration after treatment with guanidine‐hydrochloride and a reducing agent, dithiothreitol. An elution profile very similar to that of human amyloid fibrils, having protein AA as a major component, was obtained. The mink amyloid protein eluted at a position similar to that of human protein AA was by amino acid composition and partial sequence studies shown to be very similar to the latter protein and was called mink protein AA. In addition, a protein AA‐related component (protein SAA) was found in increased amounts in serum of amyloidotic mink, providing further evidence of the homology with human amy‐loidosis. Experimental amyloidosis in mink represents a suitable model for studying amyloid proteins and related serum components.