title: The primary structure of equine serum amyloid A (SAA) protein.
abstract: The complete amino acid sequence of equine serum amyloid A (SAA) was elucidated. The protein consists of 110 amino acid residues and contains an 8-amino acid residue insertion tentatively located between positions 69 and 70, as compared with human SAA. Microheterogeneities were detected at positions 16, 44, and 59, compatible with the existence of more than one SAA gene in the horse. This corresponds to the situation in man and mouse. Pronounced homology with SAA from man and several animal species was observed, thus confirming the conserved structure of this acute phase reactant and apoprotein of high-density lipoprotein (HDL).
authors.affiliation: Institute of Biochemistry, University of Oslo, Norway.
authors.forename: K
authors.initials: K
authors.lastname: Sletten
authors.forename: A
authors.initials: A
authors.lastname: Husebekk
authors.forename: G
authors.initials: G
authors.lastname: Husby
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D000882:Haplorhini; D006736:Horses / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008907:Mink; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D000685:Serum Amyloid A Protein / Q000235:genetics*
chemical_list: D000685:Serum Amyloid A Protein