The single proline‐glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A‐II
Authors:
- 20 October 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 207 (1) , 23-27
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 amyloidogenesis.Keywords
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