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Characterization of High Molecular Weight Amyloid A Proteins
Author(s) -
PRELLI F.,
PRAS M.,
SHTRASBURG S.,
FRANGIONE B.
Publication year - 1991
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.1365-3083.1991.tb02553.x
Subject(s) - edman degradation , biochemistry , protein primary structure , chemistry , serum amyloid a , amyloid (mycology) , peptide sequence , molecular mass , amino acid residue , apolipoprotein b , residue (chemistry) , amino acid , amyloid precursor protein , microbiology and biotechnology , enzyme , biology , gene , alzheimer's disease , inorganic chemistry , cholesterol , immunology , inflammation , medicine , disease , pathology
Human amyloid A protein (AA) is usually composed of the NH 2 ‐terminal 76 amino acid residue of serum amyloid A protein (SAA), although lower and higher molecular weight fragments have been reported. We studied the primary structure of six AA proteins with molecular weights of 11 kDA‐15kDA. as determined by SDS‐PAGE. Automated Edman degradation of the intact purified proteins and sequence analysis of enzymatic peptides revealed that the AA proteins were composed of only 74 to 87 residues. Moreover, fragments of apolipoprotein E or histones 2a, 3 and 4 were associated with these AA molecules. Thus, AA heterogeneity may reflect diverse processing of the SAA precursor and a very close association with other proteins.