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Characterization of Amyloid of Ageing Obese–Hyperglycaemic Mice and their Lean Littermates
Author(s) -
WESTERMARK P.,
SLETTEN K.,
NAESER P.,
NATVIG J. B.
Publication year - 1979
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.1365-3083.1979.tb02722.x
Subject(s) - amyloidosis , amyloid (mycology) , amyloid fibril , amino acid , antiserum , protein subunit , endocrinology , fibril , ageing , medicine , chemistry , peptide sequence , biochemistry , disease , antibody , pathology , immunology , amyloid β , gene
Amyloid fibrits, isolated from 18‐month‐old obese–hyperglycaemic mice and their lean littermates, were characterized immunologically and chemically. The main amyloid fibril subunit protein was protein AA, which cross‐reacted completely with an antiserum against amyloid from mice with experimentally induced amyloidosis and had an amino acid composition and N‐terminal amino acid sequence identical to that protein. These results indicate that the spontaneously occurring amyloidosis in obese–hyperglycaemic mice and their lean littermates corresponds to human, secondary amyloidosis and may serve as a model for that disease.