The Complete Amino Acid Sequence of Bovine Serum Amyloid Protein A (SAA) and of Subspecies of the Tissue-Deposited Amyloid Fibril Protein A
Autor: | Gunnar Husby, Gunilla T. Westermark, Per Westermark, Anne Husebekk, Knut Sletten, P. K. Andresen, K. Rossevatn, K. Nordstoga, Kenneth H. Johnson |
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Rok vydání: | 1992 |
Předmět: |
Molecular Sequence Data
Immunology Sequence alignment Biology Kidney Sequence Homology Nucleic Acid Animals Humans Amino Acid Sequence Serum amyloid A Bovine serum albumin Mastitis Bovine Peptide sequence Chromatography High Pressure Liquid Serum Amyloid A Protein chemistry.chemical_classification Protein primary structure General Medicine Peptide Fragments Amino acid Biochemistry chemistry Chromatography Gel biology.protein Cattle Female Lipoproteins HDL Protein A Sequence Alignment |
Zdroj: | Scandinavian Journal of Immunology. 35:217-224 |
ISSN: | 1365-3083 0300-9475 |
DOI: | 10.1111/j.1365-3083.1992.tb02853.x |
Popis: | Bovine serum amyloid A (SAA) was isolated from the acute phase high density lipoprotein (HDL) fraction of a cow suffering from acute mastitis. The elucidated primary structure revealed a protein consisting of 112 amino acid residues. Compared with SAA proteins from other species, the bovine protein was shown to have an insertion of nine amino acid residues between positions 69 and 70. No microheterogeneity could be observed in the protein. Amyloid fibrils extracted from the kidneys were found to contain at least three subspecies of protein AA, consisting of 68, 81 and about 110 amino acid residues. The amino acid sequences established for the protein AA subspecies revealed no microheterogeneity, and were identical to that elucidated for protein SAA. |
Databáze: | OpenAIRE |
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