The Primary Structure of Amyloid Fibril Protein AA in Endotoxin-Induced Amyloidosis of the Mink
| Autor: | Kristian Waalen, Gunnar Husby, Knut Nordstoga, Knut Sletten |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Amyloid
Carboxylic acid Biochemistry Species Specificity biology.animal medicine Animals Humans Amino Acid Sequence Cyanogen Bromide Mink Peptide sequence chemistry.chemical_classification Antiserum Serum Amyloid A Protein biology Amyloidosis Protein primary structure Haplorhini medicine.disease Molecular biology Peptide Fragments Amino acid Amyloid A Protein Ducks Liver chemistry |
| Zdroj: | European Journal of Biochemistry. 104:407-412 |
| ISSN: | 1432-1033 0014-2956 |
| Popis: | Two AA proteins were isolated from the same amyloid fibril preparation from the liver of a mink, in which amyloidosis had been induced by injections with endotoxin. The two proteins were of dif- ferent size, one containing 53 amino acid residues and the other 64 residues. The amino acid sequence was otherwise found to be identical. Both proteins revealed pyrrolidone carboxylic acid as the N- terminal amino acid. Sequence homologies with protein AA from other species were very striking. However, no antigenic cross-reaction was seen between mink protein AA and antisera to protein AA from human, mouse or rabbit sources. |
| Databáze: | OpenAIRE |
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