期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1980
卷号：77
期号：11
页码：6860-6864
DOI：10.1073/pnas.77.11.6860
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
