Eriksen N, Benditt E P
Proc Natl Acad Sci U S A. 1980 Nov;77(11):6860-4. doi: 10.1073/pnas.77.11.6860.
Two apoproteins immunologically related to the 9000-dalton abnormal tissue constituent known as amyloid protein AA were isolated from the lipoprotein density interval 1.125-1.21 g/cm3 (HDL3) of a pool of human serums by delipidation, gel filtration, and ion-exchange chromatography. Lesser amounts of the same apoproteins were isolated from the density interval 1.063-1.125 g/cm3 (HDL2). These apoproteins, designated apoSAA1 and apoSAA2, have molecular weights near 11,500, almost identical amino acid compositions, and slightly different isoelectric points. Their amino acid sequences are identical as far as determined (30 residues), except that apoSAA2 lacks the NH2-terminal arginine found in apoSAA1. The sequence is homologous with that of amyloid protein AA, which thus has residing in the plasma high density lipoproteins a potential precursor whose biological significance and function remain to be determined.
通过脱脂、凝胶过滤和离子交换色谱法，从一组人血清的脂蛋白密度区间1.125 - 1.21 g/cm³（HDL3）中分离出两种与被称为淀粉样蛋白AA的9000道尔顿异常组织成分具有免疫相关性的载脂蛋白。从密度区间1.063 - 1.125 g/cm³（HDL2）中分离出的相同载脂蛋白数量较少。这些载脂蛋白被命名为apoSAA1和apoSAA2，分子量接近11,500，氨基酸组成几乎相同，等电点略有不同。就已确定的部分（30个残基）而言，它们的氨基酸序列相同，只是apoSAA2缺少apoSAA1中存在的NH2末端精氨酸。该序列与淀粉样蛋白AA的序列同源，因此血浆高密度脂蛋白中存在一种潜在的前体，其生物学意义和功能尚待确定。
