Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual.
Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual.
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来自单个个体的多种形式的淀粉样蛋白相关血清蛋白 SAA 的氨基酸结构。
DOI:
10.1021/bi00405a044
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发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Benson,MD
中科院分区:
文献类型:
--
作者:
Dwulet,FE;Wallace,DK;Benson,MD
Revised Manuscript Received October 30, 1987 abstract: Multiple forms of the acute-phase serum protein SAA were isolated from the lipoprotein fraction of plasma from a single individual. These protein forms were purified bysize-exclusion, ion-exchange, and reverse-phase high-pressure liquid chromatography, and then the tryptic peptides were subjected to amino acid sequence analysis. A total of three distinct 104-residue proteins were identified. Two of these proteins differed only by having either an arginine or a histidine at position 71 while the third protein had seven amino acid differences. Each of these proteins has a 103-residue companion protein where theamino-terminal arginine has been removed. Two of these protein sequences match the two human SAA cDNA structures reported in the literature. The presence of three unique amino acid sequences in one individual is proof that there must be a minimum of two genes for SAA inhumans.