High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II.
The primary structure of a murine senile amyloid protein (ASSAM) was determined. The protein consists of a single polypeptide chain of 78 amino acid residues. The amino-terminus is blocked with pyrrolidone-carboxylic acid. The sequence differs from that of the known murine amyloid A protein and is highly homologous to human apolipoprotein (apo) A-II. The result indicates that the putative precursor of the senile amyloid protein is apo A-II in mice.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000032:analysis* / Q000096:biosynthesis; D000818:Animals; D016633:Apolipoprotein A-II; D001054:Apolipoproteins A / Q000032:analysis*; D006801:Humans; D051379:Mice
D000596:Amino Acids; D000682:Amyloid; D016633:Apolipoprotein A-II; D001054:Apolipoproteins A; C037229:amyloid fibril protein AS-SAM