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Characterization of Amyloid Protein AA and Its Serum Precursor SAA in the Horse
- Source :
- Scandinavian Journal of Immunology. 23:703-709
- Publication Year :
- 1986
- Publisher :
- Wiley, 1986.
-
Abstract
- Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to be of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to antigenicity and the 10 first N-terminal amino acid residues that have been studied up to now. The bulk of SAA was present in the high-density lipoprotein complex in serum. Also SAA was heterogeneous with respect to size, most molecules having a molecular weight of 11,000, and a minority 9000.
- Subjects :
- Amyloid
Antigenicity
Immunology
Species Specificity
medicine
Animals
Amino Acid Sequence
Horses
chemistry.chemical_classification
Serum Amyloid A Protein
Molecular mass
biology
Chemistry
Amyloidosis
General Medicine
medicine.disease
Amino acid
Molecular Weight
Liver
Biochemistry
biology.protein
Horse Diseases
Bacterial antigen
Antibody
Lipoprotein
Subjects
Details
- ISSN :
- 13653083 and 03009475
- Volume :
- 23
- Database :
- OpenAIRE
- Journal :
- Scandinavian Journal of Immunology
- Accession number :
- edsair.doi.dedup.....f1138694b81c5a4828b45a60b40d9ce3