The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II

FEBS Lett. 1986 Oct 20;207(1):23-7. doi: 10.1016/0014-5793(86)80006-0.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Amyloid / analysis*
  • Amyloid / biosynthesis
  • Animals
  • Apolipoprotein A-II
  • Apolipoproteins A / analysis*
  • Apolipoproteins A / metabolism
  • Glutamine / analysis
  • Male
  • Mice
  • Mice, Inbred ICR
  • Proline / analysis

Substances

  • Amino Acids
  • Amyloid
  • Apolipoprotein A-II
  • Apolipoproteins A
  • amyloid fibril protein AS-SAM
  • Glutamine
  • Proline