Anders R F, Natvig J B, Sletten K, Husby G, Nordstoga K
J Immunol. 1977 Jan;118(1):229-34.
The amyloid-relates serum protein SAA has been isolated by gel filtration in 10% formic acid from three animal species: mink, mouse, rabbit. Sera used in the isolation procedure were obtained from animals in which high concentrations of SAA had been induced by treatment with LPS. The isolated SAA proteins had a subunit size similar to that of human SAA, with m.w. values ranging from 10,000 to 11,700 (estimated by gel filtration in 6 M guanidine-HC1) or 12,400 to 15,000 (estimated by SDS-PAGE). The m.w. studies and amino acid sequence data indicated that SAA and the amyloid fibril protein AA in the mouse, and probably also the mink, are related in the same way as in man, the two proteins having common NH2-terminal amino acid sequences and SAA being extended by 20 to 40 residues at the COOH-terminal end of the molecule.
通过在10%甲酸中进行凝胶过滤,已从三种动物物种(水貂、小鼠、兔子)中分离出与淀粉样蛋白相关的血清蛋白SAA。分离过程中使用的血清取自经脂多糖处理诱导产生高浓度SAA的动物。分离出的SAA蛋白的亚基大小与人SAA相似,其分子量值在10,000至11,700之间(通过在6 M盐酸胍中进行凝胶过滤估算)或12,400至15,000之间(通过SDS-PAGE估算)。分子量研究和氨基酸序列数据表明,小鼠以及可能还有水貂体内的SAA和淀粉样纤维蛋白AA与人类的情况相似,这两种蛋白具有相同的NH2末端氨基酸序列,且SAA在分子的COOH末端延伸了20至40个残基。