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The single proline‐glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A‐II
Author(s) -
Higuchi Keiichi,
Yonezu Tomonori,
Tsunasawa Susumu,
Sakiyama Fumio,
Takeda Toshio
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80006-0
Subject(s) - glutamine , chemistry , proline , antigenicity , biochemistry , amino acid , amyloid (mycology) , fibril , peptide sequence , apolipoprotein b , stereochemistry , antibody , biology , cholesterol , gene , inorganic chemistry , immunology
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 (AS SAM ), which has a common antigenicity with apo A‐II. Substitution of glutamine (as sam ) for proline (apo A‐II) at position 5 is distinct and may possibly be related to murine senile amyloidogenesis.