title: The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II.
abstract: The primary structure of murine apolipoprotein A-II (apo A-II) has been determined. Apo A-II consists of a single polypeptide chain of 78 amino acid residues, of which the amino-terminus is pyrrolidone carboxylic acid. Except for residues 5 and 38, the amino acid sequence is identical to that of murine senile amyloid protein (ASSAM), which has a common antigenicity with apo A-II. Substitution of glutamine (ASSAM) for proline (apo A-II) at position 5 is distinct and may possibly be related to murine senile amyloid-ogenesis.
mesh_terms: 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* / Q000378:metabolism; D005973:Glutamine / Q000032:analysis; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D011392:Proline / Q000032:analysis
chemical_list: D000596:Amino Acids; D000682:Amyloid; D016633:Apolipoprotein A-II; D001054:Apolipoproteins A; C037229:amyloid fibril protein AS-SAM; D005973:Glutamine; D011392:Proline