The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II
| Autor: | Susumu Tsunasawa, Fumio Sakiyama, Keiichi Higuchi, Toshio Takeda, Tomonori Yonezu |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Male
Amyloid Proline Apolipoprotein B Glutamine Carboxylic acid Biophysics Primary structure Fibril Biochemistry Mice chemistry.chemical_compound Proline-glutamine substitution Biosynthesis Structural Biology Genetics Animals Amino Acid Sequence Amino Acids Molecular Biology Peptide sequence Apolipoproteins A chemistry.chemical_classification Mice Inbred ICR biology Murine senile amyloid protein Protein primary structure Cell Biology chemistry biology.protein lipids (amino acids peptides and proteins) Apolipoprotein A-II |
| Zdroj: | FEBS Letters. (1):23-27 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)80006-0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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